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Dept: Chemistry and Biochemistry  Level: masters  Country:

You searched for subject:(K Law General ). Showing records 1 – 3 of 3 total matches.

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University of Windsor

1. Mousa (Al-Ansari), Mohammad. Removal of various aromatic compounds from synthetic and refinery wastewater using soybean peroxidase.

Degree: MS, Chemistry and Biochemistry, 2008, University of Windsor

Crude soybean peroxidase (SBP), isolated from soybean seed hulls, catalyzed the oxidative polymerization of hazardous aqueous pollutant aryldiamines, aryldiols, 2-mercaptobenzothiazole and phenol in the presence of hydrogen peroxide. Experiments were conducted to investigate the optimum operating conditions including pH, hydrogen peroxide-to-substrate concentration ratio and the minimum SBP concentration required to achieve at least 95 conversion of these pollutants in synthetic and refinery wastewaters. In addition, the effect of PEG3350 on enhancing the conversion efficiency was studied. The substrate conversion and hydrogen peroxide consumption were monitored over the period of the reactions. The enzymatically-generated polymeric products from aryldiamines could be removed with surfactant, sodium dodecyl sulphate (SDS), whereas polyvalent metal cation salt, aluminium sulphate (Alum), was able to remove the products from aryldiols. Enzyme-catalyzed polymerization using SBP and the methods for removal of the generated polymeric products can provide an alternative means to the conventional treatment methods for treating aromatic wastewater pollutants. Advisors/Committee Members: Taylor, Keith (Chemistry & Biochemistry).

Subjects/Keywords: Biochemistry; General.

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APA (6th Edition):

Mousa (Al-Ansari), M. (2008). Removal of various aromatic compounds from synthetic and refinery wastewater using soybean peroxidase. (Masters Thesis). University of Windsor. Retrieved from https://scholar.uwindsor.ca/etd/3322

Chicago Manual of Style (16th Edition):

Mousa (Al-Ansari), Mohammad. “Removal of various aromatic compounds from synthetic and refinery wastewater using soybean peroxidase.” 2008. Masters Thesis, University of Windsor. Accessed November 17, 2019. https://scholar.uwindsor.ca/etd/3322.

MLA Handbook (7th Edition):

Mousa (Al-Ansari), Mohammad. “Removal of various aromatic compounds from synthetic and refinery wastewater using soybean peroxidase.” 2008. Web. 17 Nov 2019.

Vancouver:

Mousa (Al-Ansari) M. Removal of various aromatic compounds from synthetic and refinery wastewater using soybean peroxidase. [Internet] [Masters thesis]. University of Windsor; 2008. [cited 2019 Nov 17]. Available from: https://scholar.uwindsor.ca/etd/3322.

Council of Science Editors:

Mousa (Al-Ansari) M. Removal of various aromatic compounds from synthetic and refinery wastewater using soybean peroxidase. [Masters Thesis]. University of Windsor; 2008. Available from: https://scholar.uwindsor.ca/etd/3322


University of Windsor

2. Liwak, Urszula. Toxoplasma gondii Differentiation: Effects of Modifying Lactate Dehydrogenase and Argonaute Expression Patterns.

Degree: MS, Chemistry and Biochemistry, 2009, University of Windsor

Conversion between two growth stages, tachyzoites and bradyzoites, plays a key role in the pathogenesis of Toxoplasma gondii. Current studies aimed to elucidate the roles of lactate dehydrogenase (TgLDH) and argonaute (TgAgo) in relation to conversion. The over-expression of TgLDH1 or TgLDH2 did not change the overall enzymatic activity or increase growth of tachyzoites. However, a significant in vitro differentiation into bradyzoites was detected. These findings suggest that TgLDH1 and TgLDH2 have important physiological functions, in addition to being glycolytic enzymes and differentiation markers. Furthermore, altered TgAgo expression increased bradyzoite formation and interfered with the parasite’s ability to successfully perform double stranded induced gene silencing. The change in TgAgo expression also affected the levels of putative dicer proteins suggesting a direct correlation between TgAgo and an RNAi-like mechanism. Advisors/Committee Members: Ananvoranich, Sirinart (Chemistry & Biochemistry).

Subjects/Keywords: Biochemistry; General.

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APA (6th Edition):

Liwak, U. (2009). Toxoplasma gondii Differentiation: Effects of Modifying Lactate Dehydrogenase and Argonaute Expression Patterns. (Masters Thesis). University of Windsor. Retrieved from https://scholar.uwindsor.ca/etd/306

Chicago Manual of Style (16th Edition):

Liwak, Urszula. “Toxoplasma gondii Differentiation: Effects of Modifying Lactate Dehydrogenase and Argonaute Expression Patterns.” 2009. Masters Thesis, University of Windsor. Accessed November 17, 2019. https://scholar.uwindsor.ca/etd/306.

MLA Handbook (7th Edition):

Liwak, Urszula. “Toxoplasma gondii Differentiation: Effects of Modifying Lactate Dehydrogenase and Argonaute Expression Patterns.” 2009. Web. 17 Nov 2019.

Vancouver:

Liwak U. Toxoplasma gondii Differentiation: Effects of Modifying Lactate Dehydrogenase and Argonaute Expression Patterns. [Internet] [Masters thesis]. University of Windsor; 2009. [cited 2019 Nov 17]. Available from: https://scholar.uwindsor.ca/etd/306.

Council of Science Editors:

Liwak U. Toxoplasma gondii Differentiation: Effects of Modifying Lactate Dehydrogenase and Argonaute Expression Patterns. [Masters Thesis]. University of Windsor; 2009. Available from: https://scholar.uwindsor.ca/etd/306


University of Windsor

3. Mucaki, Eliseos John. Functional characterization of the interaction between heat shock protein 70 and the human dual-specificity phosphatase YVH1.

Degree: MS, Chemistry and Biochemistry, 2008, University of Windsor

YVH1 (DUSP12) is a highly conserved atypical dual-specificity phosphatase. Yeast deletion studies have suggested YVH1 plays a role in cell growth. However, the physiological role of the human orthologue is unknown. Our lab has determined that hYVH1 interacts with HSP70, a heat shock protein that plays a cell survival role. The focus of this study was to further characterize this interaction, and attempt to determine its functional significance. Results determined that this interaction is mediated through the ATPase domain of HSP70 and requires the zinc binding domain of hYVH1. Moreover, hYVH1 was found to be uncompetitively inhibited by ATP. Functional examination determined that catalytic activity of each enzyme is not affected by this interaction. Evidence suggests that over-expression of hYVH1 alters the localization of HSP70 during heat stress. Therefore, our results suggest that the HSP70-hYVH1 interaction may be critical for positioning these cell survival proteins during times of cellular stress. Advisors/Committee Members: Vacratsis, Panayiotis (Chemistry & Biochemistry).

Subjects/Keywords: Biochemistry; General.

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

APA (6th Edition):

Mucaki, E. J. (2008). Functional characterization of the interaction between heat shock protein 70 and the human dual-specificity phosphatase YVH1. (Masters Thesis). University of Windsor. Retrieved from https://scholar.uwindsor.ca/etd/2171

Chicago Manual of Style (16th Edition):

Mucaki, Eliseos John. “Functional characterization of the interaction between heat shock protein 70 and the human dual-specificity phosphatase YVH1.” 2008. Masters Thesis, University of Windsor. Accessed November 17, 2019. https://scholar.uwindsor.ca/etd/2171.

MLA Handbook (7th Edition):

Mucaki, Eliseos John. “Functional characterization of the interaction between heat shock protein 70 and the human dual-specificity phosphatase YVH1.” 2008. Web. 17 Nov 2019.

Vancouver:

Mucaki EJ. Functional characterization of the interaction between heat shock protein 70 and the human dual-specificity phosphatase YVH1. [Internet] [Masters thesis]. University of Windsor; 2008. [cited 2019 Nov 17]. Available from: https://scholar.uwindsor.ca/etd/2171.

Council of Science Editors:

Mucaki EJ. Functional characterization of the interaction between heat shock protein 70 and the human dual-specificity phosphatase YVH1. [Masters Thesis]. University of Windsor; 2008. Available from: https://scholar.uwindsor.ca/etd/2171

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