subject:(Oxidases)

Oregon State University

1. Liang, Xi. Mechanistic probes and inhibitors of L-pipecolate oxidase.

Degree: MS, Pharmacy, 1996, Oregon State University

URL: http://hdl.handle.net/1957/34088

Subjects/Keywords: Oxidases

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APA (6^th Edition):

Liang, X. (1996). Mechanistic probes and inhibitors of L-pipecolate oxidase. (Masters Thesis). Oregon State University. Retrieved from http://hdl.handle.net/1957/34088

Chicago Manual of Style (16^th Edition):

Liang, Xi. “Mechanistic probes and inhibitors of L-pipecolate oxidase.” 1996. Masters Thesis, Oregon State University. Accessed January 22, 2021. http://hdl.handle.net/1957/34088.

MLA Handbook (7^th Edition):

Liang, Xi. “Mechanistic probes and inhibitors of L-pipecolate oxidase.” 1996. Web. 22 Jan 2021.

Vancouver:

Liang X. Mechanistic probes and inhibitors of L-pipecolate oxidase. [Internet] [Masters thesis]. Oregon State University; 1996. [cited 2021 Jan 22]. Available from: http://hdl.handle.net/1957/34088.

Council of Science Editors:

Liang X. Mechanistic probes and inhibitors of L-pipecolate oxidase. [Masters Thesis]. Oregon State University; 1996. Available from: http://hdl.handle.net/1957/34088

Oregon State University

2. Kuboyama, Morio. Mammalian heart cytochrome oxidase.

Degree: PhD, Chemistry, 1964, Oregon State University

URL: http://hdl.handle.net/1957/49030

► Preparation of a cytochrome c-cytochrome oxidase complex was achieved, using crystalline beef cytochrome c and purified cytochrome oxidase from beef heart muscle, or from the… (more)

▼ Preparation of a cytochrome c-cytochrome oxidase complex was achieved, using crystalline beef cytochrome c and purified cytochrome oxidase from beef heart muscle, or from the Keilin-Hartree preparation. Succinate oxidase was reconstituted with the complex. A mixture of cytochrome oxidase, solubilized with nonionic detergent, and excess cytochrome c was exposed to sonic irradiation. The cytochrome c-cytochrome oxidase complex was isolated using gel filtration of the mixture. The ratio of the concentration of cytochrome c to cytochrome oxidase in the complex was increased with the length of sonic treatment. The complex with the maximum ratio of one was separated after a 45-60 minute period of sonic irradiation. Differential sedimentation and chromatography on Sephadex showed the complex to be an integrated entity of two components. The complex could be formed with cytochrome oxidase and either intact cytochrome c or guanidinated cytochrome c. However, both acetylated cytochrome c and succinylated cytochrome c completely failed to form any kind of complex with cytochrome oxidase. These results indicate that the interacting force between the two components is mainly electrostatic, Absolute and difference absorption spectra of the carbon monoxide compound of the complex showed a unique, distinct maximum at 415 mμ. On the other hand, a "free mixture" of both components exhibited no absorption peak at the same wave length in the presence of CO. The formation of this CO compound was prevented by sodium cholate. After separation by means of cation exchange resin, neither component of the complex showed the absorption maximum at 415 mμ in the presence of CO. From these and other observations, the possibility of a conformational change in the protein moiety of the cytochromes as a result of the interaction was hypothesized in reference to the electron transport mechanism Infrared spectrum of the complex showed no superposition of absorption bands of the two components but showed a unique band at 950 and at 1050 cm⁻¹. The physiological activity of the complex was verified by the functional reconstitution of succinate oxidase with soluble succinate dehydrogenase, the cytochrome b-c₁ particle, and the complex, The reconstituted succinate oxidase was inhibited by the usual respiratory inhibitors in the same manner as the Keilin-Hartree heart muscle preparation, the carbon monoxide inhibition of the reconstituted succinate oxidase was reversed by light. The behavior of the complex in the oxidation of ascorbate was the same as that of the heart muscle preparation. Addition of a catalytic amount of tetramethyl-p-phenylenediamine dramatically stimulated ascorbate oxidation. The cytochrome oxidase (cytochrome a plus cytochrome a₃) was functionally and structurally reconstituted from cytochrome a and intact heme a. About sixty percent of the original cytochrome oxidase activity was recovered from an incubation mixture of cytochrome a, ascorbate-EDTA, cytochrome c and hematin a. Hematin… Advisors/Committee Members: King, Tsoo E. (advisor).

Subjects/Keywords: Oxidases

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APA (6^th Edition):

Kuboyama, M. (1964). Mammalian heart cytochrome oxidase. (Doctoral Dissertation). Oregon State University. Retrieved from http://hdl.handle.net/1957/49030

Chicago Manual of Style (16^th Edition):

Kuboyama, Morio. “Mammalian heart cytochrome oxidase.” 1964. Doctoral Dissertation, Oregon State University. Accessed January 22, 2021. http://hdl.handle.net/1957/49030.

MLA Handbook (7^th Edition):

Kuboyama, Morio. “Mammalian heart cytochrome oxidase.” 1964. Web. 22 Jan 2021.

Vancouver:

Kuboyama M. Mammalian heart cytochrome oxidase. [Internet] [Doctoral dissertation]. Oregon State University; 1964. [cited 2021 Jan 22]. Available from: http://hdl.handle.net/1957/49030.

Council of Science Editors:

Kuboyama M. Mammalian heart cytochrome oxidase. [Doctoral Dissertation]. Oregon State University; 1964. Available from: http://hdl.handle.net/1957/49030

Oregon State University

3. Wilson, David Franklin. The effect of alkaline pH on the succinate oxidase system of sub-mitochondrial particles from beef heart muscle.

Degree: PhD, Chemistry, 1964, Oregon State University

URL: http://hdl.handle.net/1957/48443

► The spectrophotometric method for the determination of the acid nonextractable flavin in the proteolytic digest of the trichloroacetic acid precipitate from the heart muscle preparation… (more)

▼ The spectrophotometric method for the determination of the acid nonextractable flavin in the proteolytic digest of the trichloroacetic acid precipitate from the heart muscle preparation has been examined for the interference of the degraded hemeproteins. The proteolytic digest was chromatographically separated into the heme and flavin fractions. Spectrophotometric determinations made on the separated fractions have indicated that the heme interference is negligible for the heart muscle preparation. The validity of this method has thus been demonstrated. In the course of the proteolysis, cytochrome c₁ and c are evidently degraded to hemepeptides. The spectral behavior of the hemepeptides has been presented. Based on the fluorescent characteristics of the acid non-extractable flavin, a fluorometric method has been devised. This method is approximately 100 times more sensitive than the spectrophotometric assay. Results from these two methods are in good agreement. It is suggested that the fluorometric method may be more suitable for samples containing high concentrations of pigments adsorbing in the 450-530 mu region of the spectrum. Alkaline inactivation of the succinate oxidase activity of the heart muscle preparation in the absence of substrate and presence of oxygen has been used by Keilin and King to prepare a particle which supplies all of the respiratory components except succinate dehydrogenase for reconstitution of succinate oxidase. The succinate dehydrogenase protein, as measured by its flavin coenzyme, was found to be dissociated from the particulate heart muscle preparation by alkaline treatment. The dissociation occurred at the same rate as the inactivation of the succinate oxidase. It was therefore concluded that the original site of binding of the dehydrogenase to the particle is available to bind active succinate dehydrogenase during reconstitution of the system. The inactivation of succinate oxidase under the experimental conditions used was found to follow zero order kinetics. The apparent zero order rate constant varied as the first power of the initial enzyme concentration and the second power of the hydroxyl ion concentration. The temperature dependence of the apparent zero order rate constant was complex. A mechanism is presented which is consistant with the observed kinetics. The equilibrium dissociation of the succinate oxidase system by alkaline treatment in the presence of succinate and absence of oxygen was studied using the acid nonextractable flavin content as a measure of the succinate dehydrogenase concentration. The percent of the dehydrogenase which was soluble was a linear function of the hydroxyl ion concentration and the concentration of the soluble dehydrogenase was proportional to the total concentration bound and soluble, confirming the report of King. The equilibrium constant for the dissociation decreased with increasing temperature and buffer concentration. Advisors/Committee Members: King, Tsoo E. (advisor).

Subjects/Keywords: Oxidases

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APA (6^th Edition):

Wilson, D. F. (1964). The effect of alkaline pH on the succinate oxidase system of sub-mitochondrial particles from beef heart muscle. (Doctoral Dissertation). Oregon State University. Retrieved from http://hdl.handle.net/1957/48443

Chicago Manual of Style (16^th Edition):

Wilson, David Franklin. “The effect of alkaline pH on the succinate oxidase system of sub-mitochondrial particles from beef heart muscle.” 1964. Doctoral Dissertation, Oregon State University. Accessed January 22, 2021. http://hdl.handle.net/1957/48443.

MLA Handbook (7^th Edition):

Wilson, David Franklin. “The effect of alkaline pH on the succinate oxidase system of sub-mitochondrial particles from beef heart muscle.” 1964. Web. 22 Jan 2021.

Vancouver:

Wilson DF. The effect of alkaline pH on the succinate oxidase system of sub-mitochondrial particles from beef heart muscle. [Internet] [Doctoral dissertation]. Oregon State University; 1964. [cited 2021 Jan 22]. Available from: http://hdl.handle.net/1957/48443.

Council of Science Editors:

Wilson DF. The effect of alkaline pH on the succinate oxidase system of sub-mitochondrial particles from beef heart muscle. [Doctoral Dissertation]. Oregon State University; 1964. Available from: http://hdl.handle.net/1957/48443

Michigan State University

4. Stevens, Jeffrey Bryan. Studies on the multiplicity of microsomal mixed-function oxidase.

Degree: MS, Dept. of Biochemistry, 1970, Michigan State University

URL: http://etd.lib.msu.edu/islandora/object/etd:13226

Subjects/Keywords: Oxidases

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APA (6^th Edition):

Stevens, J. B. (1970). Studies on the multiplicity of microsomal mixed-function oxidase. (Masters Thesis). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:13226

Chicago Manual of Style (16^th Edition):

Stevens, Jeffrey Bryan. “Studies on the multiplicity of microsomal mixed-function oxidase.” 1970. Masters Thesis, Michigan State University. Accessed January 22, 2021. http://etd.lib.msu.edu/islandora/object/etd:13226.

MLA Handbook (7^th Edition):

Stevens, Jeffrey Bryan. “Studies on the multiplicity of microsomal mixed-function oxidase.” 1970. Web. 22 Jan 2021.

Vancouver:

Stevens JB. Studies on the multiplicity of microsomal mixed-function oxidase. [Internet] [Masters thesis]. Michigan State University; 1970. [cited 2021 Jan 22]. Available from: http://etd.lib.msu.edu/islandora/object/etd:13226.

Council of Science Editors:

Stevens JB. Studies on the multiplicity of microsomal mixed-function oxidase. [Masters Thesis]. Michigan State University; 1970. Available from: http://etd.lib.msu.edu/islandora/object/etd:13226

5. João Vitor Pelizzari. Presença e atividade da proteína quiescina sulfidril oxidase em sorofetal e neonatal.

Degree: 2005, Pontifícia Universidade Católica do Paraná

URL: http://www.biblioteca.pucpr.br/tede//tde_busca/arquivo.php?codArquivo=376

►

A produção de espécies reativas, particularmente de oxigênio e nitrogênio, durante o desenvolvimento embrionário e fetal tem sido bastante demonstrada nos últimos anos. Dentre essas… (more)

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A produção de espécies reativas, particularmente de oxigênio e nitrogênio, durante o desenvolvimento embrionário e fetal tem sido bastante demonstrada nos últimos anos. Dentre essas espécies, destacam-se o ânion radical superóxido, o peróxido de hidrogênio e o radical óxido nítrico produzidos enzimaticamente. O controle bem regulado da produção destas espécies garante as concentrações adequadas necessárias para o processo. Além disso, o sistema antioxidante conta com biomoléculas redutoras e enzimas, sendo aquelas pertencentes à superfamília da tiorredoxina essenciais para a manutenção do estado redox dependente do equilíbrio tiol-dissulfeto. De fato, a deleção dos genes das tiorredoxinas 1 e 2 mostrou-se letal para embriões murinos. A quiescina sulfidril oxidase (QSOX) é uma tiol oxidase cuja função não está ainda definida e que catalisa a formação de pontes dissulfetos e de peróxido de hidrogênio. Sua expressão tem sido reportada em alguns tecidos embrionários e fetais. Neste trabalho, investigamos sua presença e atividade sulfidril oxidase em soros fetal e pós-natal, em modelo bovino. Foi observada uma quantidade expressiva da proteína no soro fetal bovino e quantidades pós-natal decrescentes em soros de bezerros. A identificação da QSOX foi inequivocamente caracterizada por Western blotting. A atividade sulfidril oxidase, determinada pela produção de peróxido de hidrogênio, correlacionou-se com os níveis de expressão. Estes dados sugerem um possível papel redox dependente da QSOX na modulação do processo de desenvolvimento.

Production of reactive oxygen and nitrogen species during embryonic and fetal development has been demonstrated in the last few years. Among these species, superoxide radical anion, hydrogen peroxide and nitric oxide radical, enzymatically produced, have been considered. Their tightly controlled production provides the adequate concentrations necessary for the developmental process. In addition, the antioxidant system consists of reducing biomolecules and enzymes, particularly those belonging to the thioredoxin superfamily, which are essential to the thiol-disulfide equilibrium-dependent redox state. Indeed, knockout of the thioredoxins-1 and -2 genes are lethal for murine embryos. Quiescin sulfhydryl oxidase (QSOX) is a thiol oxidase, whose function has not been established, that catalyzes disulfide bridges and hydrogen peroxide formation. Its expression in some fetal and embryonic tissues has been reported. In this project, we analyzed QSOX presence and activity in bovine fetal and neonatal sera. A high level of QSOX was found in fetal serum, which decreases with age. QSOX identity was unequivocally characterized by Western blotting. Sulfhydryl oxidase activity, determined by hydrogen peroxide production rate, correlated with its expression levels. These data suggest a possible QSOX-dependent redox role in the modulation of developmental programs.

Advisors/Committee Members: Lia Sumie Nakao.

Subjects/Keywords: MEDICINA; Soro; Oxidases

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APA (6^th Edition):

Pelizzari, J. V. (2005). Presença e atividade da proteína quiescina sulfidril oxidase em sorofetal e neonatal. (Thesis). Pontifícia Universidade Católica do Paraná. Retrieved from http://www.biblioteca.pucpr.br/tede//tde_busca/arquivo.php?codArquivo=376

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Pelizzari, João Vitor. “Presença e atividade da proteína quiescina sulfidril oxidase em sorofetal e neonatal.” 2005. Thesis, Pontifícia Universidade Católica do Paraná. Accessed January 22, 2021. http://www.biblioteca.pucpr.br/tede//tde_busca/arquivo.php?codArquivo=376.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Pelizzari, João Vitor. “Presença e atividade da proteína quiescina sulfidril oxidase em sorofetal e neonatal.” 2005. Web. 22 Jan 2021.

Vancouver:

Pelizzari JV. Presença e atividade da proteína quiescina sulfidril oxidase em sorofetal e neonatal. [Internet] [Thesis]. Pontifícia Universidade Católica do Paraná; 2005. [cited 2021 Jan 22]. Available from: http://www.biblioteca.pucpr.br/tede//tde_busca/arquivo.php?codArquivo=376.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Pelizzari JV. Presença e atividade da proteína quiescina sulfidril oxidase em sorofetal e neonatal. [Thesis]. Pontifícia Universidade Católica do Paraná; 2005. Available from: http://www.biblioteca.pucpr.br/tede//tde_busca/arquivo.php?codArquivo=376

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Tasmania

6. Williams, Elizabeth Anne. Factors affecting alpha-acid oxidase activity in hops, Humulus lupulus L.

Degree: 1988, University of Tasmania

URL: https://eprints.utas.edu.au/21902/1/whole_WilliamsElizabethAnne1990_thesis.pdf

Subjects/Keywords: Hops; Oxidases

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APA (6^th Edition):

Williams, E. A. (1988). Factors affecting alpha-acid oxidase activity in hops, Humulus lupulus L. (Thesis). University of Tasmania. Retrieved from https://eprints.utas.edu.au/21902/1/whole_WilliamsElizabethAnne1990_thesis.pdf

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Williams, Elizabeth Anne. “Factors affecting alpha-acid oxidase activity in hops, Humulus lupulus L.” 1988. Thesis, University of Tasmania. Accessed January 22, 2021. https://eprints.utas.edu.au/21902/1/whole_WilliamsElizabethAnne1990_thesis.pdf.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Williams, Elizabeth Anne. “Factors affecting alpha-acid oxidase activity in hops, Humulus lupulus L.” 1988. Web. 22 Jan 2021.

Vancouver:

Williams EA. Factors affecting alpha-acid oxidase activity in hops, Humulus lupulus L. [Internet] [Thesis]. University of Tasmania; 1988. [cited 2021 Jan 22]. Available from: https://eprints.utas.edu.au/21902/1/whole_WilliamsElizabethAnne1990_thesis.pdf.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Williams EA. Factors affecting alpha-acid oxidase activity in hops, Humulus lupulus L. [Thesis]. University of Tasmania; 1988. Available from: https://eprints.utas.edu.au/21902/1/whole_WilliamsElizabethAnne1990_thesis.pdf

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Michigan State University

7. Cheng, Greg. Shu-Guang. Studies on xanthine oxidase in cow's milk.

Degree: PhD, Department of Food Science and Human Nutrition, 1983, Michigan State University

URL: http://etd.lib.msu.edu/islandora/object/etd:34245

Subjects/Keywords: Oxidases; Milk

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APA (6^th Edition):

Cheng, G. S. (1983). Studies on xanthine oxidase in cow's milk. (Doctoral Dissertation). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:34245

Chicago Manual of Style (16^th Edition):

Cheng, Greg Shu-Guang. “Studies on xanthine oxidase in cow's milk.” 1983. Doctoral Dissertation, Michigan State University. Accessed January 22, 2021. http://etd.lib.msu.edu/islandora/object/etd:34245.

MLA Handbook (7^th Edition):

Cheng, Greg Shu-Guang. “Studies on xanthine oxidase in cow's milk.” 1983. Web. 22 Jan 2021.

Vancouver:

Cheng GS. Studies on xanthine oxidase in cow's milk. [Internet] [Doctoral dissertation]. Michigan State University; 1983. [cited 2021 Jan 22]. Available from: http://etd.lib.msu.edu/islandora/object/etd:34245.

Council of Science Editors:

Cheng GS. Studies on xanthine oxidase in cow's milk. [Doctoral Dissertation]. Michigan State University; 1983. Available from: http://etd.lib.msu.edu/islandora/object/etd:34245

Montana State University

8. Hystad, Steven Michael. The genetic characterization of a nil polyphenol oxidase (PPO) trait for the improvement of end product quality in wheat (Triticum aestivum).

Degree: MS, College of Agriculture, 2014, Montana State University

URL: https://scholarworks.montana.edu/xmlui/handle/1/9359

► Wheat (Triticum aestivum) polyphenol oxidase (PPO) contributes to the time dependent discoloration of Asian noodles. Wheat contains multiple paralogous and orthologous PPO genes expressed in… (more)

▼ Wheat (Triticum aestivum) polyphenol oxidase (PPO) contributes to the time dependent discoloration of Asian noodles. Wheat contains multiple paralogous and orthologous PPO genes expressed in wheat kernels, Ppo-A1, Ppo-D1, Ppo-A2, Ppo-D2, and Ppo-B2. To date, wheat improvement efforts have focused on breeding cultivars containing Ppo-D1 and Ppo-A1 alleles conferring reduced PPO activity. A major impediment to wheat quality improvement is a lack of additional PPO alleles conferring reduced kernel PPO. Thus, the discovery of novel low or null PPO alleles is critical to further reduce PPO and improve noodle color stability. The objective of this study was to 1) Characterize mutations present in a low PPO line 07OR1074 and create molecular markers associated with newly characterized alleles; 2) assess the allelic impact of the newly characterized alleles on kernel PPO activity and upon Chinese white salted noodle quality. To characterize additional mutations present and develop molecular markers, genomic clones were created for each known PPO gene and sequenced. Previously reported very low PPO line, 07OR1074, was found to contain a novel allele at Ppo-A2 and null alleles at Ppo-A1 and Ppo-D1 loci and molecular markers were created that encompassed each mutation. To determine the allelic impact of the new alleles on kernel PPO activity, F3:4 lines were genotyped with the novel molecular markers, grown in the field in Bozeman, Montana, and assayed for kernel PPO activity. Evaluation of lines indicated a substantial genotypic effect on PPO with Ppo-A1 and Ppo-D1 loci contributing significantly (P <.001) to total PPO. To determine the effect of the null PPO alleles upon noodle quality Chinese white salted noodles were produced from both refined white flour and whole wheat flour. The results clearly demonstrate that the null PPO alleles at Ppo-A1 and Ppo-D1 loci produce noodles that are brighter (greater L*), more red (greater a*), and more yellow (greater b*) at 24 and 48 hours. These results show that mutations in Ppo-A1 and Ppo-D1 genes are important to lowering overall wheat kernel PPO activity producing a more desirable and marketable product. Advisors/Committee Members: Chairperson, Graduate Committee: Michael J. Giroux (advisor).

Subjects/Keywords: Wheat.; Polyphenols.; Oxidases.; Noodles.

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APA (6^th Edition):

Hystad, S. M. (2014). The genetic characterization of a nil polyphenol oxidase (PPO) trait for the improvement of end product quality in wheat (Triticum aestivum). (Masters Thesis). Montana State University. Retrieved from https://scholarworks.montana.edu/xmlui/handle/1/9359

Chicago Manual of Style (16^th Edition):

Hystad, Steven Michael. “The genetic characterization of a nil polyphenol oxidase (PPO) trait for the improvement of end product quality in wheat (Triticum aestivum).” 2014. Masters Thesis, Montana State University. Accessed January 22, 2021. https://scholarworks.montana.edu/xmlui/handle/1/9359.

MLA Handbook (7^th Edition):

Hystad, Steven Michael. “The genetic characterization of a nil polyphenol oxidase (PPO) trait for the improvement of end product quality in wheat (Triticum aestivum).” 2014. Web. 22 Jan 2021.

Vancouver:

Hystad SM. The genetic characterization of a nil polyphenol oxidase (PPO) trait for the improvement of end product quality in wheat (Triticum aestivum). [Internet] [Masters thesis]. Montana State University; 2014. [cited 2021 Jan 22]. Available from: https://scholarworks.montana.edu/xmlui/handle/1/9359.

Council of Science Editors:

Hystad SM. The genetic characterization of a nil polyphenol oxidase (PPO) trait for the improvement of end product quality in wheat (Triticum aestivum). [Masters Thesis]. Montana State University; 2014. Available from: https://scholarworks.montana.edu/xmlui/handle/1/9359

Rhodes University

9. Simpson, Clinton. Isolation, purification and characterization of a novel glucose oxidase from Penicillium canescens Tt42.

Degree: Faculty of Science, Biochemistry, Microbiology and Biotechnology;, 2006, Rhodes University

URL: http://hdl.handle.net/10962/d1004034

► A novel glucose oxidase from Penicillium canescens (Tt42) was isolated, purified and characterised. The P. canescens Tt42 was cultivated using an optimised growth medium from… (more)

▼ A novel glucose oxidase from Penicillium canescens (Tt42) was isolated, purified and characterised. The P. canescens Tt42 was cultivated using an optimised growth medium from literature, and maximum glucose oxidase activities of 11.5 U/ml and 6.9 U/ml for the intra- and extracellular fractions were obtained. Maximum glucose oxidase production was achieved after 72 hours at 28°C which coincided with glucose depletion. A total of 1104 U (from 60ml) of glucose oxidase was produced with a biomass specific glucose oxidase activity of 1.08 Umg[superscript -1] Four methods of cell disruption were evaluated for release of intracellular glucose oxidase from P. canescens Tt42 cells. These methods were; sonication, French press, Freeze-Thaw and a high pressure cell disrupter (Z-Plus Series) from Constant systems. All the methods were successful in releasing the intracellular glucose oxidase from P. canescens Tt42. The use of the Constant Systems high pressure cell disrupter was preferred, since it was the simplest and most rapid method. Ammonium sulphate precipitation was shown to be effective as an initial purification step for extracellular glucose oxidase from P. canescens Tt42. Comparison of the intra- and extracellular glucose oxidase fractions using isoelectric focusing showed 2 isoenzymes in both fractions. The pI values of the isoenzymes were determined to be 4.30 and 4.67, with the former being dominant. Since both the intra- and extracellular fractions contained the same isoenzymes of glucose oxidase, further purification studies were performed using the extracellular fraction. The glucose oxidase from P. canescens Tt42 was purified using 3 main techniques: ammonium sulphate precipitation (60% - 70% cut), anion exchange chromatography (Super Q 650M) and size exclusion chromatography (Sephadex S200HR). The glucose oxidase was determined to be ±80% pure by size exclusion chromatography. The final purified glucose oxidase was lyophilised, and an overall purification yield of 10.3% was achieved with an 8.6-fold purification. The purified glucose oxidase was confirmed to be catalase free. Glucose oxidase from P. canescens Tt42 was determined to be a dimeric protein (M[subscript r] ±148kDa) likely consisting of 2 equal subunits (M[subscript r] ± 70kDa). The temperature optimum range was shown to be 25-30°C. The optimum pH for the oxidation of β-D-glucose was pH 7. The enzyme was shown to be stable at 25°C for 10 hours, with a half life of approximately 30 minutes at 37°C. The lyophilised enzyme was stable at -20°C for 6 months. The properties of glucose oxidase from Tt42 were comparable to alternative glucose oxidase enzymes from Aspergillus and other Penicillium species. Glucose oxidase from P. canescens Tt42 was shown to have distinct kinetic characteristics. The V[subscript max] and K[subscript m] were shown to be 651 Umg[superscript -1] and 18.4 mM towards β-D-glucose. The catalytic kcat and specificity k[subscript cat]/K[subscript m] constants for glucose oxidase from P. canescens Tt42 were shown to be 791…

Subjects/Keywords: Penicillium; Glucose; Oxidases

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APA (6^th Edition):

Simpson, C. (2006). Isolation, purification and characterization of a novel glucose oxidase from Penicillium canescens Tt42. (Thesis). Rhodes University. Retrieved from http://hdl.handle.net/10962/d1004034

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Simpson, Clinton. “Isolation, purification and characterization of a novel glucose oxidase from Penicillium canescens Tt42.” 2006. Thesis, Rhodes University. Accessed January 22, 2021. http://hdl.handle.net/10962/d1004034.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Simpson, Clinton. “Isolation, purification and characterization of a novel glucose oxidase from Penicillium canescens Tt42.” 2006. Web. 22 Jan 2021.

Vancouver:

Simpson C. Isolation, purification and characterization of a novel glucose oxidase from Penicillium canescens Tt42. [Internet] [Thesis]. Rhodes University; 2006. [cited 2021 Jan 22]. Available from: http://hdl.handle.net/10962/d1004034.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Simpson C. Isolation, purification and characterization of a novel glucose oxidase from Penicillium canescens Tt42. [Thesis]. Rhodes University; 2006. Available from: http://hdl.handle.net/10962/d1004034

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Illinois – Urbana-Champaign

10. Miner, Kyle D. Rational design of functional heme copper oxidases in myoglobin.

Degree: PhD, 0318, 2012, University of Illinois – Urbana-Champaign

URL: http://hdl.handle.net/2142/29570

► Proteins are involved in nearly every process that occurs in living systems, either as a main participant in the process or preforming a supporting role.… (more)

▼ Proteins are involved in nearly every process that occurs in living systems, either as a main participant in the process or preforming a supporting role. It is estimated that approximately half of proteins in living systems are associated with a metal in some fashion. With such a high percentage of proteins interacting with metals, it may not be a surprise that most cellular pathways that have at least one metalloprotein performing one or more steps. Many, if not all, of the most important and complex processes that occur in living systems are performed by a metalloprotein. These processes include photosynthesis, cellular respiration, and nucleic acid repair. The metals in these proteins expand the potential chemistry beyond what can be done with only the 20 naturally occurring amino acids. However, nature uses relatively few metal complexes, such as heme cofactors or iron sulfur clusters or metal ions, considering the number of functions that metalloproteins perform. Also, nature uses a surprisingly small number of protein domains and folds compared the number of possible folds. In metalloproteins, both the metal and protein environment surrounding it play an important role in determining the chemistry that is performed. The protein adjusts the properties of the metal, such as the redox potential or the number of open coordination sites. Many metal ions found in metalloproteins are less reactive outside of a protein environment. Despite many years of study, we are only beginning to understand the functioning of large complex metalloproteins, such as heme copper oxidases (HCOs) in respiration or the oxygen evolving complex in photosystems. Large complex proteins pose two problems with respect to studying function. Large complexes are relatively difficult to isolate in a biologically relevant form and the multiple metal sites can either interfere with spectroscopic analysis or require the use of relatively sophisticated methodology. As an alternative to studying these complex proteins, we have chosen instead to redesign an existing well-studied heme protein, myoglobin, to mimic the bimetallic, heme-CuB site of HCOs. This is the site where molecular oxygen is converted to water as part of cellular respiration. The conversion of oxygen to water is highly difficult as there are many highly reactive intermediates that must stabilized so that the reaction can result in water formation. Such a redesign can be thought of as going from the “bottom up” with respect to the desired function. In the process of building up such a model, we are producing minimalistic versions in order to see what the function of each of the structural features is and how it affects chemistry. This thesis describes the improvement of an existing myoglobin based model system of HCOs, named CuBMb, where an non-native copper site was previously engineered into myoglobin by adding two histidine residues. Along with the native histidine, the resulting site resembles the CuB site found in HCOs. This model protein is purified without metal in the CuB… Advisors/Committee Members: Lu, Yi (advisor), Lu, Yi (Committee Chair), Cronan, John E. (committee member), Gennis, Robert B. (committee member), Rienstra, Chad M. (committee member).

Subjects/Keywords: Protein Design; Heme Copper Oxidases; Enzyme modeling

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APA (6^th Edition):

Miner, K. D. (2012). Rational design of functional heme copper oxidases in myoglobin. (Doctoral Dissertation). University of Illinois – Urbana-Champaign. Retrieved from http://hdl.handle.net/2142/29570

Chicago Manual of Style (16^th Edition):

Miner, Kyle D. “Rational design of functional heme copper oxidases in myoglobin.” 2012. Doctoral Dissertation, University of Illinois – Urbana-Champaign. Accessed January 22, 2021. http://hdl.handle.net/2142/29570.

MLA Handbook (7^th Edition):

Miner, Kyle D. “Rational design of functional heme copper oxidases in myoglobin.” 2012. Web. 22 Jan 2021.

Vancouver:

Miner KD. Rational design of functional heme copper oxidases in myoglobin. [Internet] [Doctoral dissertation]. University of Illinois – Urbana-Champaign; 2012. [cited 2021 Jan 22]. Available from: http://hdl.handle.net/2142/29570.

Council of Science Editors:

Miner KD. Rational design of functional heme copper oxidases in myoglobin. [Doctoral Dissertation]. University of Illinois – Urbana-Champaign; 2012. Available from: http://hdl.handle.net/2142/29570

University of Arizona

11. Kipke, Cary Alan. Physical studies and synthetic modeling of the molybdenum-containing enzyme sulfite oxidase.

Degree: 1988, University of Arizona

URL: http://hdl.handle.net/10150/184456

► This research has been directed at the study of both the enzyme sulfite oxidase and molybdenum model chemistry. A modification of a previously published procedure… (more)

▼ This research has been directed at the study of both the enzyme sulfite oxidase and molybdenum model chemistry. A modification of a previously published procedure has been used to purify sulfite oxidase in high yield which is well-suited for experiments requiring prosthetically intact enzyme and which is not contaminated with extraneous heme or with other redox active proteins. Laser flash photolysis was used to study the reaction of photoproduced 5-deazariboflavin, lumiflavin, and riboflavin semiquinone radicals with the redox centers of purified sulfite oxidase. Two distinctly different intramolecular electron transfer processes were observed between the molybdenum and heme sites of the enzyme, and these assignments were supported by flash photolysis studies of the cyanide-inactivated enzyme and the sulfite oxidase heme peptide. Microcoulometric experiments on sulfite oxidase have shown that the enzyme requires the addition of three electrons for complete subunit reduction. Midpoint potentials for the Mo(VI)/Mo(V), Mo(V)/Mo(IV), and Fe(III)/Fe(II) couples have been obtained under varied buffer conditions. The midpoint potentials obtained under High-pH and Low-pH conditions provided a means for reductively titrating the enzyme to the Mo(V) oxidation state for EXAFS studies. EXAFS of sulfite oxidase under High-pH and Low-pH conditions have provided the first example of a structural study of the three accessible oxidation states (Mo(VI), Mo(V), and Mo(IV)). A biologically relevant synthetic model for the formation of the Mo(V) Low-pH form of sulfite oxidase has been developed. The Mo(V) model compound closely resembles the minimum coordination environment for the Mo(V) Low-pH form of sulfite oxidase as determined by EXAFS. Using synchrotron radiation, molybdenum L-edge x-ray absorption spectra have been obtained for a variety of oxomolybdenum(V) compounds which serve as models for sulfite oxidase. An attempt has been made to correlate unique features of the molecules to the observed 2P → 4d electronic transitions.

Subjects/Keywords: Molybdenum enzymes.; Oxidases.

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APA (6^th Edition):

Kipke, C. A. (1988). Physical studies and synthetic modeling of the molybdenum-containing enzyme sulfite oxidase. (Doctoral Dissertation). University of Arizona. Retrieved from http://hdl.handle.net/10150/184456

Chicago Manual of Style (16^th Edition):

Kipke, Cary Alan. “Physical studies and synthetic modeling of the molybdenum-containing enzyme sulfite oxidase. ” 1988. Doctoral Dissertation, University of Arizona. Accessed January 22, 2021. http://hdl.handle.net/10150/184456.

MLA Handbook (7^th Edition):

Kipke, Cary Alan. “Physical studies and synthetic modeling of the molybdenum-containing enzyme sulfite oxidase. ” 1988. Web. 22 Jan 2021.

Vancouver:

Kipke CA. Physical studies and synthetic modeling of the molybdenum-containing enzyme sulfite oxidase. [Internet] [Doctoral dissertation]. University of Arizona; 1988. [cited 2021 Jan 22]. Available from: http://hdl.handle.net/10150/184456.

Council of Science Editors:

Kipke CA. Physical studies and synthetic modeling of the molybdenum-containing enzyme sulfite oxidase. [Doctoral Dissertation]. University of Arizona; 1988. Available from: http://hdl.handle.net/10150/184456

Brock University

12. Hill, Bruce. Reactivity characteristics of cytochrome c, cytochrome oxidase and the electrostatic cytochrome c - cytochrome oxidase complex .

Degree: Department of Biological Sciences, 1979, Brock University

URL: http://hdl.handle.net/10464/1572

► The mechanism whereby cytochrome £ oxidase catalyses elec-. tron transfer from cytochrome £ to oxygen remains an unsolved problem. Polarographic and spectrophotometric activity measurements of… (more)

▼ The mechanism whereby cytochrome £ oxidase catalyses elec-. tron transfer from cytochrome £ to oxygen remains an unsolved problem. Polarographic and spectrophotometric activity measurements of purified, particulate and soluble forms of beef heart mitochondrial cytochrome c oxidase presented in this thesis confirm the following characteristics of the steady-state kinetics with respect to cytochrome £: (1) oxidation of ferrocytochrome c is first order under all conditions. -(2) The relationship between sustrate concentration and velocity is of the Michaelis-Menten type over a limited range of substrate. concentrations at high ionic strength. (3) ~he reaction rate is independent from oxygen concentration until very low levels of oxygen. (4) "Biphasic" kinetic plots of enzyme activity as a function of substrate concentration are found when the range of cytochrome c concentrations is extended; the biphasicity ~ is more apparent in low ionic strength buffer. These results imply two binding sites for cytochrome £ on the oxidase; one of high affinity and one of low affinity with Km values of 1.0 pM and 3.0 pM, respectively, under low ionic strength conditions. (5) Inhibition of the enzymic rate by azide is non-c~mpetitive with respect to cytochrome £ under all conditions indicating an internal electron transfer step, and not binding or dissociation of £ from the enzyme is rate limiting. The "tight" binding of cytochrome '£ to cytochrome c oxidase is confirmed in column chromatographic experiments. The complex has a cytochrome £:oxidase ratio of 1.0 and is dissociated in media of high ionic strength. Stopped-flow spectrophotometric studies of the reduction of equimolar mixtures and complexes of cytochrome c and the oxidase were initiated in an attempt to assess the functional relevance of such a complex. Two alternative routes -for reduction of the oxidase, under conditions where the predominant species is the £ - aa3 complex, are postulated; (i) electron transfer via tightly bound cytochrome £, (ii) electron transfer via a small population of free cytochrome c interacting at the "loose" binding site implied from kinetic studies. It is impossible to conclude, based on the results obtained, which path is responsible for the reduction of cytochrome a. The rate of reduction by various reductants of free cytochrome £ in high and low ionic strength and of cytochrome £ electrostatically bound to cytochrome oxidase was investigated. Ascorbate, a negatively charged reagent, reduces free cytochrome £ with a rate constant dependent on ionic strength, whereas neutral reagents TMPD and DAD were relatively unaffected by ionic strength in their reduction of cytochrome c. The zwitterion cysteine behaved similarly to uncharged reductants DAD and TI~PD in exhibiting only a marginal response to ionic strength. Ascorbate reduces bound cytochrome £ only slowly, but DAD and TMPD reduce bound cytochrome £ rapidly. Reduction of cytochrome £ by DAD and TMPD in the £ - aa3 complex was enhanced…

Subjects/Keywords: Cytochrome c.; Oxidases.

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APA (6^th Edition):

Hill, B. (1979). Reactivity characteristics of cytochrome c, cytochrome oxidase and the electrostatic cytochrome c - cytochrome oxidase complex . (Thesis). Brock University. Retrieved from http://hdl.handle.net/10464/1572

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Hill, Bruce. “Reactivity characteristics of cytochrome c, cytochrome oxidase and the electrostatic cytochrome c - cytochrome oxidase complex .” 1979. Thesis, Brock University. Accessed January 22, 2021. http://hdl.handle.net/10464/1572.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Hill, Bruce. “Reactivity characteristics of cytochrome c, cytochrome oxidase and the electrostatic cytochrome c - cytochrome oxidase complex .” 1979. Web. 22 Jan 2021.

Vancouver:

Hill B. Reactivity characteristics of cytochrome c, cytochrome oxidase and the electrostatic cytochrome c - cytochrome oxidase complex . [Internet] [Thesis]. Brock University; 1979. [cited 2021 Jan 22]. Available from: http://hdl.handle.net/10464/1572.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Hill B. Reactivity characteristics of cytochrome c, cytochrome oxidase and the electrostatic cytochrome c - cytochrome oxidase complex . [Thesis]. Brock University; 1979. Available from: http://hdl.handle.net/10464/1572

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Sydney

13. Stangenberg, Stefanie. Fetal programming of chronic kidney disease and novel treatment targets of renal fibrosis .

Degree: 2017, University of Sydney

URL: http://hdl.handle.net/2123/17744

► The thesis spans the spectrum of causative and therapeutic aspects of chronic kidney disease (CKD), which is a significant and growing health burden. An adverse… (more)

▼ The thesis spans the spectrum of causative and therapeutic aspects of chronic kidney disease (CKD), which is a significant and growing health burden. An adverse in utero environment is increasingly recognised to predispose to chronic diseases in adulthood. Maternal smoking remains the most common modifiable adverse in-utero exposure leading to low birth weight, which is strongly associated with CKD in later life. In order to investigate underlying mechanisms for such susceptibility, a mouse model of maternal smoke exposure was used and the offspring examined at different developmental milestones. Maternal smoke exposure led to lower birth weight and increased proteinuria at adulthood compared to control. From birth throughout adulthood smoke exposed offspring had increased levels of mitochondria-derived oxidative stress and increased mitochondrial DNA copy numbers. In addition, the kidneys of smoke exposed offspring demonstrated mitochondrial structural abnormalities at birth and adulthood along with a reduction in oxidative phosphorylation (OXPHOS) proteins, lysosome density and mitochondrial antioxidants. The development of mitochondrial alterations preceding the proteinuria may point towards its mechanistic role in fetal programming of CKD in response to maternal smoking. While it is desirable that these findings will translate into effective strategies of CKD prevention, the disease is frequently diagnosed when renal fibrosis has already developed. Thus, the second part of this thesis focused on therapy and explored whether lysyl oxidase-like 2 (LOXL2), an enzyme central to extracellular matrix modification (ECM), would be suitable as a novel treatment target. LOXL2 was increased in early renal fibrosis after unilateral ureteral obstruction and in a diabetic mouse model that mimics the development of chronic renal fibrosis. Inhibition of LOXL2 with a highly selective, small molecule inhibitor reduced markers of ECM deposition in the diabetic mouse model. Importantly, LOXL2 inhibition resulted in amelioration of proteinuria and glomerulosclerosis in the diabetic mice. It thus had a beneficial effect on preserving glomerular structure and function. We conclude that it may be a suitable therapeutic target in diabetic nephropathy and renal fibrosis of other aetiologies.

Subjects/Keywords: fetal programming; renal fibrosis; lysyl; oxidases

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APA (6^th Edition):

Stangenberg, S. (2017). Fetal programming of chronic kidney disease and novel treatment targets of renal fibrosis . (Thesis). University of Sydney. Retrieved from http://hdl.handle.net/2123/17744

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Stangenberg, Stefanie. “Fetal programming of chronic kidney disease and novel treatment targets of renal fibrosis .” 2017. Thesis, University of Sydney. Accessed January 22, 2021. http://hdl.handle.net/2123/17744.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Stangenberg, Stefanie. “Fetal programming of chronic kidney disease and novel treatment targets of renal fibrosis .” 2017. Web. 22 Jan 2021.

Vancouver:

Stangenberg S. Fetal programming of chronic kidney disease and novel treatment targets of renal fibrosis . [Internet] [Thesis]. University of Sydney; 2017. [cited 2021 Jan 22]. Available from: http://hdl.handle.net/2123/17744.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Stangenberg S. Fetal programming of chronic kidney disease and novel treatment targets of renal fibrosis . [Thesis]. University of Sydney; 2017. Available from: http://hdl.handle.net/2123/17744

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

The Ohio State University

14. Fry, David William. Purification and characterization of glycolic acid oxidase and glycolic acid dehydrogenase from human liver.

Degree: PhD, Graduate School, 1977, The Ohio State University

URL: http://rave.ohiolink.edu/etdc/view?acc_num=osu1487005965827788

Subjects/Keywords: Chemistry; Dehydrogenases; Oxidases

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APA (6^th Edition):

Fry, D. W. (1977). Purification and characterization of glycolic acid oxidase and glycolic acid dehydrogenase from human liver. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1487005965827788

Chicago Manual of Style (16^th Edition):

Fry, David William. “Purification and characterization of glycolic acid oxidase and glycolic acid dehydrogenase from human liver.” 1977. Doctoral Dissertation, The Ohio State University. Accessed January 22, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487005965827788.

MLA Handbook (7^th Edition):

Fry, David William. “Purification and characterization of glycolic acid oxidase and glycolic acid dehydrogenase from human liver.” 1977. Web. 22 Jan 2021.

Vancouver:

Fry DW. Purification and characterization of glycolic acid oxidase and glycolic acid dehydrogenase from human liver. [Internet] [Doctoral dissertation]. The Ohio State University; 1977. [cited 2021 Jan 22]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1487005965827788.

Council of Science Editors:

Fry DW. Purification and characterization of glycolic acid oxidase and glycolic acid dehydrogenase from human liver. [Doctoral Dissertation]. The Ohio State University; 1977. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1487005965827788

University of Manchester

15. Brzezniak, Agata. Exploiting Transaminases and Amine Oxidases for the Synthesis of Enantiomerically Pure Compounds of Biological Relevance.

Degree: 2019, University of Manchester

URL: http://www.manchester.ac.uk/escholar/uk-ac-man-scw:318487

► Efficient generation of amine-bearing privileged structures represents a cornerstone of modern organic chemistry. Such compounds can be employed for the preparation of drug targets or… (more)

▼ Efficient generation of amine-bearing privileged structures represents a cornerstone of modern organic chemistry. Such compounds can be employed for the preparation of drug targets or compound libraries suitable for biological screening. Application of biocatalysis in organic synthesis allows for a more sustainable manufacture of enantiomerically pure privileged scaffolds. The key aim of this research project was to utilise the existing toolbox of transaminase and monoamine oxidase enzymes in the preparation of biologically important compounds. Firstly, chiral key amine intermediates were successfully obtained in high yields and enantiomeric excess from biotransformations of (S)-selective ATA-113 and MAO-N D9 enzyme variants, which allowed for the subsequent synthesis of JAK2/STAT3 signalling pathway inhibitors. The resulting racemic, (S)- and (R)- configured alkyne analogues of WP1066 were evaluated for their biological activities including the determination of their anti-proliferative activities against aggressive MDA- MB-231 breast cancer cell line (IC50 = ~600 nM for all variants). Secondly, the chemoenzymatic approach to hygrine and tropinone natural products was attempted using putrescine transaminase and monoamine oxidase biocatalysts, respectively. The dehydrohygrine framework was the unexpected product resulting from monoamine oxidase oxidation of hygrine. Additionally, quinolizidine scaffolds present in xestospongin and petrosin natural products were synthesised using the Polonovski-Potier reaction and their tertiary amine precursors were screened against existing amine oxidases. Lastly, a keramaphidin B analogue was successfully synthesised using a biomimetic approach providing evidence for the manzamine biosynthesis hypothesis. The potential of amine oxidase biocatalysts was also further demonstrated in the preparation of the same keramaphidin B framework using a biocatalytic methodology. Advisors/Committee Members: TURNER, NICHOLAS NJ, Whitehead, Roger, Turner, Nicholas.

Subjects/Keywords: amine oxidases; transaminases; biocatalysis; manzamine; hygrine; petrosin; xestospongin; WP1066; DUBs; monoamine oxidases; MAO-N

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APA (6^th Edition):

Brzezniak, A. (2019). Exploiting Transaminases and Amine Oxidases for the Synthesis of Enantiomerically Pure Compounds of Biological Relevance. (Doctoral Dissertation). University of Manchester. Retrieved from http://www.manchester.ac.uk/escholar/uk-ac-man-scw:318487

Chicago Manual of Style (16^th Edition):

Brzezniak, Agata. “Exploiting Transaminases and Amine Oxidases for the Synthesis of Enantiomerically Pure Compounds of Biological Relevance.” 2019. Doctoral Dissertation, University of Manchester. Accessed January 22, 2021. http://www.manchester.ac.uk/escholar/uk-ac-man-scw:318487.

MLA Handbook (7^th Edition):

Brzezniak, Agata. “Exploiting Transaminases and Amine Oxidases for the Synthesis of Enantiomerically Pure Compounds of Biological Relevance.” 2019. Web. 22 Jan 2021.

Vancouver:

Brzezniak A. Exploiting Transaminases and Amine Oxidases for the Synthesis of Enantiomerically Pure Compounds of Biological Relevance. [Internet] [Doctoral dissertation]. University of Manchester; 2019. [cited 2021 Jan 22]. Available from: http://www.manchester.ac.uk/escholar/uk-ac-man-scw:318487.

Council of Science Editors:

Brzezniak A. Exploiting Transaminases and Amine Oxidases for the Synthesis of Enantiomerically Pure Compounds of Biological Relevance. [Doctoral Dissertation]. University of Manchester; 2019. Available from: http://www.manchester.ac.uk/escholar/uk-ac-man-scw:318487

University of Manchester

16. Brzezniak, Agata. Exploiting transaminases and amine oxidases for the synthesis of enantiomerically pure compounds of biological relevance.

Degree: PhD, 2019, University of Manchester

URL: https://www.research.manchester.ac.uk/portal/en/theses/exploiting-transaminases-and-amine-oxidases-for-the-synthesis-of-enantiomerically-pure-compounds-of-biological-relevance(90d98172-bc4e-4f42-914c-d55f06f2a242).html ; https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.799439

► Efficient generation of amine-bearing privileged structures represents a cornerstone of modern organic chemistry. Such compounds can be employed for the preparation of drug targets or… (more)

Subjects/Keywords: MAO-N; monoamine oxidases; DUBs; WP1066; xestospongin; hygrine; manzamine; biocatalysis; transaminases; amine oxidases; petrosin

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APA (6^th Edition):

Brzezniak, A. (2019). Exploiting transaminases and amine oxidases for the synthesis of enantiomerically pure compounds of biological relevance. (Doctoral Dissertation). University of Manchester. Retrieved from https://www.research.manchester.ac.uk/portal/en/theses/exploiting-transaminases-and-amine-oxidases-for-the-synthesis-of-enantiomerically-pure-compounds-of-biological-relevance(90d98172-bc4e-4f42-914c-d55f06f2a242).html ; https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.799439

Chicago Manual of Style (16^th Edition):

Brzezniak, Agata. “Exploiting transaminases and amine oxidases for the synthesis of enantiomerically pure compounds of biological relevance.” 2019. Doctoral Dissertation, University of Manchester. Accessed January 22, 2021. https://www.research.manchester.ac.uk/portal/en/theses/exploiting-transaminases-and-amine-oxidases-for-the-synthesis-of-enantiomerically-pure-compounds-of-biological-relevance(90d98172-bc4e-4f42-914c-d55f06f2a242).html ; https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.799439.

MLA Handbook (7^th Edition):

Brzezniak, Agata. “Exploiting transaminases and amine oxidases for the synthesis of enantiomerically pure compounds of biological relevance.” 2019. Web. 22 Jan 2021.

Vancouver:

Brzezniak A. Exploiting transaminases and amine oxidases for the synthesis of enantiomerically pure compounds of biological relevance. [Internet] [Doctoral dissertation]. University of Manchester; 2019. [cited 2021 Jan 22]. Available from: https://www.research.manchester.ac.uk/portal/en/theses/exploiting-transaminases-and-amine-oxidases-for-the-synthesis-of-enantiomerically-pure-compounds-of-biological-relevance(90d98172-bc4e-4f42-914c-d55f06f2a242).html ; https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.799439.

Council of Science Editors:

Brzezniak A. Exploiting transaminases and amine oxidases for the synthesis of enantiomerically pure compounds of biological relevance. [Doctoral Dissertation]. University of Manchester; 2019. Available from: https://www.research.manchester.ac.uk/portal/en/theses/exploiting-transaminases-and-amine-oxidases-for-the-synthesis-of-enantiomerically-pure-compounds-of-biological-relevance(90d98172-bc4e-4f42-914c-d55f06f2a242).html ; https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.799439

17. Zhong, Bo. Mechanism-based Inhibitors for Copper Amine Oxidases: Synthesis, Mechanism, and Enzymology.

Degree: PhD, Chemistry, 2010, Case Western Reserve University School of Graduate Studies

URL: http://rave.ohiolink.edu/etdc/view?acc_num=case1259013895

► Development of mechanism-based inhibitors and the related inhibition mechanism study have always been significant studies in the field of copper amine oxidases (CAOs). In… (more)

▼ Development of mechanism-based inhibitors and the related inhibition mechanism study have always been significant studies in the field of copper amine oxidases (CAOs). In Chapter 2, synthesis of several analogs of 1-amino-2,3-butadiene, which contain mono- or disubstitution at C4, and screening against bovine plasma amine oxidase (BPAO) and Arthrobacter globiformis amine oxidase (AGAO) are described. In the case of AGAO, the crystal structure of the enzyme derivitized with 6-phenylhexa-2,3-dienylamine has been obtained. This structure reveals the covalent attachment of the aldehyde product generated from amine oxidation to the amino group of the reduced TPQ cofactor. In Chapter 3, evaluation as inhibitor of BPAO of a novel activated allylamine derivative acetic acid-3-amino-propenyl ester is described. Both the E- and Z-isomers display two modes of inactivation of BPAO, reversible and irreversible. In the reversible inactivation pathway, (E)-acetic acid-3-amino-propenyl ester (1) acts as a substrate of BPAO to induce the temporary reversible inactivation of BPAO. A new inactivation mechanism was proposed for the permanent inactivation of BPAO by (E)-acetic acid-3-amino-propenyl ester (1), which involves hydrolysis of product Schiff base at the ester bond followed by tautomerizaiton of TPQ adduct I to II (hydrolysis-tautomerization mechanism). In Chapter 4, kinetic analyse of propargylamine derivatives 4-phenoxy-2-butynamine (PBA) and 4-(4-methylphenoxy)-2-butynamine (MPBA) as both substrates and inhibitors of BPAO is described. The substrate activity, the inhibitory activity, and the corresponding α-C deuterium isotope effects on both activities were determined for both compounds vs. BPAO. To obtain further insights into the inactivation mechanism, the inactivation of the native BPAO and the substrate-reduced BPAO by the turnover product α, β-unsaturated aldehydes was evaluated. The results can be reconciled by a mechanism where the turnover product α, β-unsaturated aldehyde forms an adduct with the amino group of the reduced TPQ cofactor. In Chapter 5, synthesis of several Ar-X-extended derivatives of homopropargylamine (X=NH, O) and evaluation of them as BPAO inhibitors are described. The structural basis of inactivation was probed by UV-Vis spectrophotometric studies, mass spectrometry, and immunochemical analysis. Advisors/Committee Members: Sayre, Lawrence (Advisor), Tochtrop, Gregory (Committee Chair), Lee, Irene (Advisor).

Subjects/Keywords: BPAO; AMINE OXIDASES; OXIDASES; Inactivation; INHIBITORS; AMINE

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APA (6^th Edition):

Zhong, B. (2010). Mechanism-based Inhibitors for Copper Amine Oxidases: Synthesis, Mechanism, and Enzymology. (Doctoral Dissertation). Case Western Reserve University School of Graduate Studies. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=case1259013895

Chicago Manual of Style (16^th Edition):

Zhong, Bo. “Mechanism-based Inhibitors for Copper Amine Oxidases: Synthesis, Mechanism, and Enzymology.” 2010. Doctoral Dissertation, Case Western Reserve University School of Graduate Studies. Accessed January 22, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=case1259013895.

MLA Handbook (7^th Edition):

Zhong, Bo. “Mechanism-based Inhibitors for Copper Amine Oxidases: Synthesis, Mechanism, and Enzymology.” 2010. Web. 22 Jan 2021.

Vancouver:

Zhong B. Mechanism-based Inhibitors for Copper Amine Oxidases: Synthesis, Mechanism, and Enzymology. [Internet] [Doctoral dissertation]. Case Western Reserve University School of Graduate Studies; 2010. [cited 2021 Jan 22]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=case1259013895.

Council of Science Editors:

Zhong B. Mechanism-based Inhibitors for Copper Amine Oxidases: Synthesis, Mechanism, and Enzymology. [Doctoral Dissertation]. Case Western Reserve University School of Graduate Studies; 2010. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=case1259013895

18. Green, Edward L. Characterization of the TPQ cofactor in amine oxidases and the heme cofactor in cystathionine beta-synthase by resonance raman spectroscopy. Implications for catalytic properties.

Degree: PhD, 2001, Oregon Health Sciences University

URL: doi:10.6083/M4M906KM ; http://digitalcommons.ohsu.edu/etd/119

Subjects/Keywords: Amine oxidase; Copper enzymes; Oxidases

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Green, E. L. (2001). Characterization of the TPQ cofactor in amine oxidases and the heme cofactor in cystathionine beta-synthase by resonance raman spectroscopy. Implications for catalytic properties. (Doctoral Dissertation). Oregon Health Sciences University. Retrieved from doi:10.6083/M4M906KM ; http://digitalcommons.ohsu.edu/etd/119

Chicago Manual of Style (16^th Edition):

Green, Edward L. “Characterization of the TPQ cofactor in amine oxidases and the heme cofactor in cystathionine beta-synthase by resonance raman spectroscopy. Implications for catalytic properties.” 2001. Doctoral Dissertation, Oregon Health Sciences University. Accessed January 22, 2021. doi:10.6083/M4M906KM ; http://digitalcommons.ohsu.edu/etd/119.

MLA Handbook (7^th Edition):

Green, Edward L. “Characterization of the TPQ cofactor in amine oxidases and the heme cofactor in cystathionine beta-synthase by resonance raman spectroscopy. Implications for catalytic properties.” 2001. Web. 22 Jan 2021.

Vancouver:

Green EL. Characterization of the TPQ cofactor in amine oxidases and the heme cofactor in cystathionine beta-synthase by resonance raman spectroscopy. Implications for catalytic properties. [Internet] [Doctoral dissertation]. Oregon Health Sciences University; 2001. [cited 2021 Jan 22]. Available from: doi:10.6083/M4M906KM ; http://digitalcommons.ohsu.edu/etd/119.

Council of Science Editors:

Green EL. Characterization of the TPQ cofactor in amine oxidases and the heme cofactor in cystathionine beta-synthase by resonance raman spectroscopy. Implications for catalytic properties. [Doctoral Dissertation]. Oregon Health Sciences University; 2001. Available from: doi:10.6083/M4M906KM ; http://digitalcommons.ohsu.edu/etd/119

University of Tasmania

19. Dewar, Catharine Lynne. Studies on the granulocyte cell surface oxidase.

Degree: 1979, University of Tasmania

URL: https://eprints.utas.edu.au/19456/1/whole_DewarCatharineLynne1981_thesis.pdf

► This thesis examined the possible role of the microfilaments and microtubules in controlling the activity of the granulocyte plasma membrane oxidase. There have not been… (more)

▼ This thesis examined the possible role of the microfilaments and microtubules in controlling the activity of the granulocyte plasma membrane oxidase. There have not been any detailed investigations of this topic published to date. The conflicting literature on the nucleotide specificity and location of the oxidase within the granulocyte was examined. In vitro techniques for isolating granulocytes from human peripheral blood and for quantitating the initial rate of plasma membrane oxidase activity were developed and used for these investigations. The involvement of microfilaments and microtubules in oxidase activity was studied by using pharmacological agents known to disrupt these structures in vitro (cytochalasin B, and colchicine, vinblastine and vincristine, respectively). Control experiments were also performed to ensure that microfilament and microtubule disruption by these agents provided the best explanation for the results presented herein. Correlative experiments were conducted to determine if a change in hexose monophosphate shunt activity was associated with the observed changes in plasma membrane oxidase activity brought about by the drug treatments. Experiments on non-phagocytic granulocytes showed that microfilament disruption led to enhanced oxidase activity, while microtubule disruption produced a dual effect : a paradoxical enhancement (with low doses or brief exposures to the agents) and an impairment in oxidase activity. These results suggested that microfilaments act as a constraint against, while microtubules are required for plasma membrane oxidase activity. The requirement for microtubules was highlighted in experiments where the usual enhancement in oxidase activity with cytochalasin B was ablated when the granulocytes were concomitantly incubated with a microtubule-disrupting agent. (With phagocytic granulocytes qualitatively similar results were observed. However, those experiments were not suitable for studying cell surface oxidase activity because the presence of ingestable. Particles made it impossible to determine whether plasma membrane and/or granule oxidase activity was being measured.) Based on the spectrophotometric and electron microscopic results presented and the relevant findings from other investigators, a scheme concerning the participation of the cytoskeletal elements in granulocyte plasma membrane oxidase activity was devised. In this scheme the microfilaments physically constrain the oxidase within the plasma membrane, and thereby hold the activity of the oxidase in check. Thus, microfilament disruption is envisaged to result in enhanced oxidase activity by freeing the enzyme. However, the oxidase is viewed as optimally active only as long as the microtubules are present to maintain the plasma membrane topography suitable for the enzyme's activity.

Subjects/Keywords: Granulocytes; Cell membranes; Oxidases; Microtubules

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APA (6^th Edition):

Dewar, C. L. (1979). Studies on the granulocyte cell surface oxidase. (Thesis). University of Tasmania. Retrieved from https://eprints.utas.edu.au/19456/1/whole_DewarCatharineLynne1981_thesis.pdf

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Dewar, Catharine Lynne. “Studies on the granulocyte cell surface oxidase.” 1979. Thesis, University of Tasmania. Accessed January 22, 2021. https://eprints.utas.edu.au/19456/1/whole_DewarCatharineLynne1981_thesis.pdf.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Dewar, Catharine Lynne. “Studies on the granulocyte cell surface oxidase.” 1979. Web. 22 Jan 2021.

Vancouver:

Dewar CL. Studies on the granulocyte cell surface oxidase. [Internet] [Thesis]. University of Tasmania; 1979. [cited 2021 Jan 22]. Available from: https://eprints.utas.edu.au/19456/1/whole_DewarCatharineLynne1981_thesis.pdf.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Dewar CL. Studies on the granulocyte cell surface oxidase. [Thesis]. University of Tasmania; 1979. Available from: https://eprints.utas.edu.au/19456/1/whole_DewarCatharineLynne1981_thesis.pdf

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

20. Khan, Amjad Ali. Studies on soluble and immobilized polyphenol oxidases: applications in the decolorization and removal of aromatic dyes from polluted wastewater; -.

Degree: Biochemistry, 2005, Aligarh Muslim University

URL: http://shodhganga.inflibnet.ac.in/handle/10603/53965

Abstract not available newline newline

Summary p. 107-109, Bibliography p. 110-119

Advisors/Committee Members: Husain, Qayyum.

Subjects/Keywords: Immobilized; Polyphenol; Oxidases; Decolorization; Aromatic

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APA (6^th Edition):

Khan, A. A. (2005). Studies on soluble and immobilized polyphenol oxidases: applications in the decolorization and removal of aromatic dyes from polluted wastewater; -. (Thesis). Aligarh Muslim University. Retrieved from http://shodhganga.inflibnet.ac.in/handle/10603/53965

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Khan, Amjad Ali. “Studies on soluble and immobilized polyphenol oxidases: applications in the decolorization and removal of aromatic dyes from polluted wastewater; -.” 2005. Thesis, Aligarh Muslim University. Accessed January 22, 2021. http://shodhganga.inflibnet.ac.in/handle/10603/53965.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Khan, Amjad Ali. “Studies on soluble and immobilized polyphenol oxidases: applications in the decolorization and removal of aromatic dyes from polluted wastewater; -.” 2005. Web. 22 Jan 2021.

Vancouver:

Khan AA. Studies on soluble and immobilized polyphenol oxidases: applications in the decolorization and removal of aromatic dyes from polluted wastewater; -. [Internet] [Thesis]. Aligarh Muslim University; 2005. [cited 2021 Jan 22]. Available from: http://shodhganga.inflibnet.ac.in/handle/10603/53965.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Khan AA. Studies on soluble and immobilized polyphenol oxidases: applications in the decolorization and removal of aromatic dyes from polluted wastewater; -. [Thesis]. Aligarh Muslim University; 2005. Available from: http://shodhganga.inflibnet.ac.in/handle/10603/53965

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Rhodes University

21. Burton, Stephanie Gail. Biocatalytic and biomimetic studies of polyphenol oxidase.

Degree: PhD, Faculty of Science, Biochemistry, Microbiology and Biotechnology, 1994, Rhodes University

URL: http://hdl.handle.net/10962/d1004088

► Mushroom polyphenol oxidase (EC 1.14.18.1) was investigated to determine its potential for application as a biocatalyst in the synthesis of o-quinones, in organic medium. In… (more)

▼ Mushroom polyphenol oxidase (EC 1.14.18.1) was investigated to determine its potential for application as a biocatalyst in the synthesis of o-quinones, in organic medium. In order to determine the kinetic properties of the biocatalyst, a system was devised which comprised an immobilised polyphenol oxidase extract, functioning in chloroform. The system was hydrated by the addition of buffer. A simple method for the consistent measurement of reaction rates in this heterogenous system was designed and used to obtain detailed enzyme kinetic data relating to optimisation of reaction conditions and substrate specificity. The aqueous content of the system was optimised using p-cresol as a substrate. A crude, immobilised extract of Agaricus bisporus was used to hydroxylate and oxidise a range of selected p-substituted phenolic substrates, yielding, as the sale products, o-quinones. These products were efficiently reduced to catechols by extracting the reaction mixtures with aqueous ascorbic acid solution. The biocatalytic system was also successfully utilised to produce L-DOPA, the drug used to treat Parkinson's disease, from L-acetyl tyrosine ethyl ester (ATEE). Michaelis-Menten kinetics were used to obtain apparent Km and V values with respect to the selected phenolic substrates, and the kinetic parameters obtained were found to correlate well with the steric requirements of the substrates and with their hydrophobicity. In the course of the investigation, a novel ¹H NMR method was used to facilitate measurement of the UV molar absorption coefficients of the o-quinones in reaction mixtures, thus avoiding the necessity to isolate these unstable, water-sensitive products. The biocatalytic system was extended to a continuous process, in which the immobilised enzyme was shown to function successfully in the chloroform medium for several hours, with high conversion rates. Modifications, involving partial purification and the addition of a surfactant, were investigated to determine their effect on the kinetic parameters. The results obtained using partially purified enzyme indicated that the removal of extraneous protein and/or melanoid material lead to a reduced capacity for conversion of sterically demanding substrates. The addition of the anionic detergent, sodium dodecyl sulphate (SOS), enhanced the ability of the biocatalyst to bind and oxidise sterically demanding substrates. These effects are attributed to changes in the polar state of groups within the protein binding pocket, which result in altered flexibility and hydrophobicity. Computer modelling of several biomimetic dinuclear copper complexes also indicated the importance of flexibility for effective biocatalysis. Novel binuclear copper (II complexes, containing a flexible biphenyl spacer and imidazole or benzimidazole donors, were prepared and analysed using NMR, UV, AA and cyclic voltammetric techniques. The complexes were also shown, in a detailed kinetic study, to mimic the catecholase activity of polyphenol oxidase by oxidising 3,5-di-tertbutylcatechol, and to… Advisors/Committee Members: Duncan, John, Kaye, Perry, Rose, Peter.

Subjects/Keywords: Phenol oxidase; Polyphenols; Oxidases

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APA (6^th Edition):

Burton, S. G. (1994). Biocatalytic and biomimetic studies of polyphenol oxidase. (Doctoral Dissertation). Rhodes University. Retrieved from http://hdl.handle.net/10962/d1004088

Chicago Manual of Style (16^th Edition):

Burton, Stephanie Gail. “Biocatalytic and biomimetic studies of polyphenol oxidase.” 1994. Doctoral Dissertation, Rhodes University. Accessed January 22, 2021. http://hdl.handle.net/10962/d1004088.

MLA Handbook (7^th Edition):

Burton, Stephanie Gail. “Biocatalytic and biomimetic studies of polyphenol oxidase.” 1994. Web. 22 Jan 2021.

Vancouver:

Burton SG. Biocatalytic and biomimetic studies of polyphenol oxidase. [Internet] [Doctoral dissertation]. Rhodes University; 1994. [cited 2021 Jan 22]. Available from: http://hdl.handle.net/10962/d1004088.

Council of Science Editors:

Burton SG. Biocatalytic and biomimetic studies of polyphenol oxidase. [Doctoral Dissertation]. Rhodes University; 1994. Available from: http://hdl.handle.net/10962/d1004088

California State University – San Bernardino

22. Glinternick, Michael F. Polyphenal oxidase activity and dark pigment of oospore walls in Chara Globularis.

Degree: Biology, 1980, California State University – San Bernardino

URL: http://scholarworks.lib.csusb.edu/etd-project/193

Subjects/Keywords: Characeae; Oxidases; Plant Biology

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APA (6^th Edition):

Glinternick, M. F. (1980). Polyphenal oxidase activity and dark pigment of oospore walls in Chara Globularis. (Thesis). California State University – San Bernardino. Retrieved from http://scholarworks.lib.csusb.edu/etd-project/193

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Glinternick, Michael F. “Polyphenal oxidase activity and dark pigment of oospore walls in Chara Globularis.” 1980. Thesis, California State University – San Bernardino. Accessed January 22, 2021. http://scholarworks.lib.csusb.edu/etd-project/193.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Glinternick, Michael F. “Polyphenal oxidase activity and dark pigment of oospore walls in Chara Globularis.” 1980. Web. 22 Jan 2021.

Vancouver:

Glinternick MF. Polyphenal oxidase activity and dark pigment of oospore walls in Chara Globularis. [Internet] [Thesis]. California State University – San Bernardino; 1980. [cited 2021 Jan 22]. Available from: http://scholarworks.lib.csusb.edu/etd-project/193.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Glinternick MF. Polyphenal oxidase activity and dark pigment of oospore walls in Chara Globularis. [Thesis]. California State University – San Bernardino; 1980. Available from: http://scholarworks.lib.csusb.edu/etd-project/193

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Brigham Young University

23. Hinkson, Jimmy W. A study of three photochemical activities of chloroplasts.

Degree: MS, 1958, Brigham Young University

URL: https://scholarsarchive.byu.edu/cgi/viewcontent.cgi?article=9229&context=etd

► Chloroplasts of sugar beet leaves were subjected to treatment by heating, by incubation at pH 8.5 and pH 5.5, by incubation in ion low… (more)

Subjects/Keywords: Chromatophores; Photochemistry; Cytochromes; Oxidases; Peoxidase

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APA (6^th Edition):

Hinkson, J. W. (1958). A study of three photochemical activities of chloroplasts. (Masters Thesis). Brigham Young University. Retrieved from https://scholarsarchive.byu.edu/cgi/viewcontent.cgi?article=9229&context=etd

Chicago Manual of Style (16^th Edition):

Hinkson, Jimmy W. “A study of three photochemical activities of chloroplasts.” 1958. Masters Thesis, Brigham Young University. Accessed January 22, 2021. https://scholarsarchive.byu.edu/cgi/viewcontent.cgi?article=9229&context=etd.

MLA Handbook (7^th Edition):

Hinkson, Jimmy W. “A study of three photochemical activities of chloroplasts.” 1958. Web. 22 Jan 2021.

Vancouver:

Hinkson JW. A study of three photochemical activities of chloroplasts. [Internet] [Masters thesis]. Brigham Young University; 1958. [cited 2021 Jan 22]. Available from: https://scholarsarchive.byu.edu/cgi/viewcontent.cgi?article=9229&context=etd.

Council of Science Editors:

Hinkson JW. A study of three photochemical activities of chloroplasts. [Masters Thesis]. Brigham Young University; 1958. Available from: https://scholarsarchive.byu.edu/cgi/viewcontent.cgi?article=9229&context=etd

Hong Kong University of Science and Technology

24. Zhou, Huiqing. Structural and functional relationship of ACC synthase.

Degree: 1998, Hong Kong University of Science and Technology

URL: http://repository.ust.hk/ir/Record/1783.1-3832 ; https://doi.org/10.14711/thesis-b583781 ; http://repository.ust.hk/ir/bitstream/1783.1-3832/1/th_redirect.html

► Ethylene is a plant hormone regulating many aspects of plant growth and development, and its effects are of commercial importance in both agriculture and horticulture.… (more)

Subjects/Keywords: Carboxylic acids ; Oxidases ; Ethylene – Synthesis

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APA (6^th Edition):

Zhou, H. (1998). Structural and functional relationship of ACC synthase. (Thesis). Hong Kong University of Science and Technology. Retrieved from http://repository.ust.hk/ir/Record/1783.1-3832 ; https://doi.org/10.14711/thesis-b583781 ; http://repository.ust.hk/ir/bitstream/1783.1-3832/1/th_redirect.html

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Zhou, Huiqing. “Structural and functional relationship of ACC synthase.” 1998. Thesis, Hong Kong University of Science and Technology. Accessed January 22, 2021. http://repository.ust.hk/ir/Record/1783.1-3832 ; https://doi.org/10.14711/thesis-b583781 ; http://repository.ust.hk/ir/bitstream/1783.1-3832/1/th_redirect.html.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Zhou, Huiqing. “Structural and functional relationship of ACC synthase.” 1998. Web. 22 Jan 2021.

Vancouver:

Zhou H. Structural and functional relationship of ACC synthase. [Internet] [Thesis]. Hong Kong University of Science and Technology; 1998. [cited 2021 Jan 22]. Available from: http://repository.ust.hk/ir/Record/1783.1-3832 ; https://doi.org/10.14711/thesis-b583781 ; http://repository.ust.hk/ir/bitstream/1783.1-3832/1/th_redirect.html.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Zhou H. Structural and functional relationship of ACC synthase. [Thesis]. Hong Kong University of Science and Technology; 1998. Available from: http://repository.ust.hk/ir/Record/1783.1-3832 ; https://doi.org/10.14711/thesis-b583781 ; http://repository.ust.hk/ir/bitstream/1783.1-3832/1/th_redirect.html

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Michigan State University

25. Rhoads, David Michael. Developmental and salicylic acid regulated expression of the alternative oxidase of higher plants.

Degree: PhD, Department of Biochemistry, 1992, Michigan State University

URL: http://etd.lib.msu.edu/islandora/object/etd:21879

Subjects/Keywords: Salicylic acid; Plants – Respiration; Oxidases

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APA (6^th Edition):

Rhoads, D. M. (1992). Developmental and salicylic acid regulated expression of the alternative oxidase of higher plants. (Doctoral Dissertation). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:21879

Chicago Manual of Style (16^th Edition):

Rhoads, David Michael. “Developmental and salicylic acid regulated expression of the alternative oxidase of higher plants.” 1992. Doctoral Dissertation, Michigan State University. Accessed January 22, 2021. http://etd.lib.msu.edu/islandora/object/etd:21879.

MLA Handbook (7^th Edition):

Rhoads, David Michael. “Developmental and salicylic acid regulated expression of the alternative oxidase of higher plants.” 1992. Web. 22 Jan 2021.

Vancouver:

Rhoads DM. Developmental and salicylic acid regulated expression of the alternative oxidase of higher plants. [Internet] [Doctoral dissertation]. Michigan State University; 1992. [cited 2021 Jan 22]. Available from: http://etd.lib.msu.edu/islandora/object/etd:21879.

Council of Science Editors:

Rhoads DM. Developmental and salicylic acid regulated expression of the alternative oxidase of higher plants. [Doctoral Dissertation]. Michigan State University; 1992. Available from: http://etd.lib.msu.edu/islandora/object/etd:21879

Michigan State University

26. O'Neal, Fredrick Oliver. Carbon tetrachloride metabolism : the role of hepatic microsomal mixed-function oxidase components in carbon-halogen bond cleavage.

Degree: PhD, 1978, Michigan State University

URL: http://etd.lib.msu.edu/islandora/object/etd:21152

Subjects/Keywords: Carbon tetrachloride; Enzymes; Microsomes; Oxidases

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APA (6^th Edition):

O'Neal, F. O. (1978). Carbon tetrachloride metabolism : the role of hepatic microsomal mixed-function oxidase components in carbon-halogen bond cleavage. (Doctoral Dissertation). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:21152

Chicago Manual of Style (16^th Edition):

O'Neal, Fredrick Oliver. “Carbon tetrachloride metabolism : the role of hepatic microsomal mixed-function oxidase components in carbon-halogen bond cleavage.” 1978. Doctoral Dissertation, Michigan State University. Accessed January 22, 2021. http://etd.lib.msu.edu/islandora/object/etd:21152.

MLA Handbook (7^th Edition):

O'Neal, Fredrick Oliver. “Carbon tetrachloride metabolism : the role of hepatic microsomal mixed-function oxidase components in carbon-halogen bond cleavage.” 1978. Web. 22 Jan 2021.

Vancouver:

O'Neal FO. Carbon tetrachloride metabolism : the role of hepatic microsomal mixed-function oxidase components in carbon-halogen bond cleavage. [Internet] [Doctoral dissertation]. Michigan State University; 1978. [cited 2021 Jan 22]. Available from: http://etd.lib.msu.edu/islandora/object/etd:21152.

Council of Science Editors:

O'Neal FO. Carbon tetrachloride metabolism : the role of hepatic microsomal mixed-function oxidase components in carbon-halogen bond cleavage. [Doctoral Dissertation]. Michigan State University; 1978. Available from: http://etd.lib.msu.edu/islandora/object/etd:21152

Michigan State University

27. Reiken, Steven R. Evaluation of the co-immobilization of l-lysine alpha-oxidase and catalase in a hollow fiber reactor system.

Degree: MS, Department of Chemical Engineering, 1988, Michigan State University

URL: http://etd.lib.msu.edu/islandora/object/etd:21623

Subjects/Keywords: Lysine; Oxidases; Catalase; Immobilized enzymes

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APA (6^th Edition):

Reiken, S. R. (1988). Evaluation of the co-immobilization of l-lysine alpha-oxidase and catalase in a hollow fiber reactor system. (Masters Thesis). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:21623

Chicago Manual of Style (16^th Edition):

Reiken, Steven R. “Evaluation of the co-immobilization of l-lysine alpha-oxidase and catalase in a hollow fiber reactor system.” 1988. Masters Thesis, Michigan State University. Accessed January 22, 2021. http://etd.lib.msu.edu/islandora/object/etd:21623.

MLA Handbook (7^th Edition):

Reiken, Steven R. “Evaluation of the co-immobilization of l-lysine alpha-oxidase and catalase in a hollow fiber reactor system.” 1988. Web. 22 Jan 2021.

Vancouver:

Reiken SR. Evaluation of the co-immobilization of l-lysine alpha-oxidase and catalase in a hollow fiber reactor system. [Internet] [Masters thesis]. Michigan State University; 1988. [cited 2021 Jan 22]. Available from: http://etd.lib.msu.edu/islandora/object/etd:21623.

Council of Science Editors:

Reiken SR. Evaluation of the co-immobilization of l-lysine alpha-oxidase and catalase in a hollow fiber reactor system. [Masters Thesis]. Michigan State University; 1988. Available from: http://etd.lib.msu.edu/islandora/object/etd:21623

Michigan State University

28. Amon, Anton. Physico-chemical properties of ascorbate oxidase isozymes.

Degree: PhD, Department of Food Science, 1970, Michigan State University

URL: http://etd.lib.msu.edu/islandora/object/etd:34527

Subjects/Keywords: Ascorbate oxidase; Oxidases; Isoenzymes

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APA (6^th Edition):

Amon, A. (1970). Physico-chemical properties of ascorbate oxidase isozymes. (Doctoral Dissertation). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:34527

Chicago Manual of Style (16^th Edition):

Amon, Anton. “Physico-chemical properties of ascorbate oxidase isozymes.” 1970. Doctoral Dissertation, Michigan State University. Accessed January 22, 2021. http://etd.lib.msu.edu/islandora/object/etd:34527.

MLA Handbook (7^th Edition):

Amon, Anton. “Physico-chemical properties of ascorbate oxidase isozymes.” 1970. Web. 22 Jan 2021.

Vancouver:

Amon A. Physico-chemical properties of ascorbate oxidase isozymes. [Internet] [Doctoral dissertation]. Michigan State University; 1970. [cited 2021 Jan 22]. Available from: http://etd.lib.msu.edu/islandora/object/etd:34527.

Council of Science Editors:

Amon A. Physico-chemical properties of ascorbate oxidase isozymes. [Doctoral Dissertation]. Michigan State University; 1970. Available from: http://etd.lib.msu.edu/islandora/object/etd:34527

Michigan State University

29. Kwon, Chae-Soon. Influence of antidotes, MFO inhibitors, insecticides, and corn hybrids on ALS-inhibiting herbicide activity.

Degree: PhD, Department of Crop and Social Sciences, 1993, Michigan State University

URL: http://etd.lib.msu.edu/islandora/object/etd:24358

Subjects/Keywords: Oxidases; Hybrid corn; Insecticides; Herbicides

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APA (6^th Edition):

Kwon, C. (1993). Influence of antidotes, MFO inhibitors, insecticides, and corn hybrids on ALS-inhibiting herbicide activity. (Doctoral Dissertation). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:24358

Chicago Manual of Style (16^th Edition):

Kwon, Chae-Soon. “Influence of antidotes, MFO inhibitors, insecticides, and corn hybrids on ALS-inhibiting herbicide activity.” 1993. Doctoral Dissertation, Michigan State University. Accessed January 22, 2021. http://etd.lib.msu.edu/islandora/object/etd:24358.

MLA Handbook (7^th Edition):

Kwon, Chae-Soon. “Influence of antidotes, MFO inhibitors, insecticides, and corn hybrids on ALS-inhibiting herbicide activity.” 1993. Web. 22 Jan 2021.

Vancouver:

Kwon C. Influence of antidotes, MFO inhibitors, insecticides, and corn hybrids on ALS-inhibiting herbicide activity. [Internet] [Doctoral dissertation]. Michigan State University; 1993. [cited 2021 Jan 22]. Available from: http://etd.lib.msu.edu/islandora/object/etd:24358.

Council of Science Editors:

Kwon C. Influence of antidotes, MFO inhibitors, insecticides, and corn hybrids on ALS-inhibiting herbicide activity. [Doctoral Dissertation]. Michigan State University; 1993. Available from: http://etd.lib.msu.edu/islandora/object/etd:24358

Michigan State University

30. Green, John Henry. Comparison of soluble reduced nicotinamide adenine dinucleotide oxidases from vegetative cells and spores of Clostridium botulinum 62-A.

Degree: PhD, Department of Microbiology and Public Health, 1963, Michigan State University

URL: http://etd.lib.msu.edu/islandora/object/etd:40504

Subjects/Keywords: Oxidases; Clostridium botulinum; Cells

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APA (6^th Edition):

Green, J. H. (1963). Comparison of soluble reduced nicotinamide adenine dinucleotide oxidases from vegetative cells and spores of Clostridium botulinum 62-A. (Doctoral Dissertation). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:40504

Chicago Manual of Style (16^th Edition):

Green, John Henry. “Comparison of soluble reduced nicotinamide adenine dinucleotide oxidases from vegetative cells and spores of Clostridium botulinum 62-A.” 1963. Doctoral Dissertation, Michigan State University. Accessed January 22, 2021. http://etd.lib.msu.edu/islandora/object/etd:40504.

MLA Handbook (7^th Edition):

Green, John Henry. “Comparison of soluble reduced nicotinamide adenine dinucleotide oxidases from vegetative cells and spores of Clostridium botulinum 62-A.” 1963. Web. 22 Jan 2021.

Vancouver:

Green JH. Comparison of soluble reduced nicotinamide adenine dinucleotide oxidases from vegetative cells and spores of Clostridium botulinum 62-A. [Internet] [Doctoral dissertation]. Michigan State University; 1963. [cited 2021 Jan 22]. Available from: http://etd.lib.msu.edu/islandora/object/etd:40504.

Council of Science Editors:

Green JH. Comparison of soluble reduced nicotinamide adenine dinucleotide oxidases from vegetative cells and spores of Clostridium botulinum 62-A. [Doctoral Dissertation]. Michigan State University; 1963. Available from: http://etd.lib.msu.edu/islandora/object/etd:40504

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