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Hydrolysis of S-aryl-cysteinylglycine conjugates catalyzed by porcine kidney cortex membrane dipeptidase

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dc.contributor.advisor Josephy, P. David
dc.contributor.author Poon, James
dc.date.accessioned 2012-08-31T19:56:49Z
dc.date.available 2012-08-31T19:56:49Z
dc.date.copyright 2012-08
dc.date.created 2012-08-14
dc.date.issued 2012-08-31
dc.identifier.uri http://hdl.handle.net/10214/3897
dc.description.abstract Following conjugation with glutathione, xenobiotics are converted into cysteinylglycine conjugates, cysteine conjugates, and, finally, mercapturic acids. The structural factors determining the activities of dipeptidases for the metabolism of toxicologically-relevant cysteinylglycine conjugates are not well understood. I purified porcine kidney cortex membrane dipeptidase (MDP) to homogeneity, via phosphatidylinositol-specific phospholipase C-mediated cleavage of the protein’s membrane anchor and cilastatin affinity chromatography. The homodimeric structure of the MDP protein was confirmed by mass spectrometry. To test the enzyme activity of purified MDP, the cysteinylglycine conjugates of 1-(chloromethyl)naphthalene, 4-nitrobenzyl chloride, and 1-chloro-2,4-dinitrobenzene were synthesized and HPLC separation methods for their quantitation were developed. MDP catalyzed the hydrolysis of all three conjugates, but the rate of this activity was strongly dependent on the nature of the substituent on the cysteine sulfur atom. en_US
dc.language.iso en en_US
dc.subject cilastatin en_US
dc.subject glutathione en_US
dc.subject mercapturic acid pathway en_US
dc.subject affinity chromatography en_US
dc.subject menaphthylglutathione en_US
dc.subject dinitrophenylglutathione en_US
dc.subject enzyme kinetics en_US
dc.title Hydrolysis of S-aryl-cysteinylglycine conjugates catalyzed by porcine kidney cortex membrane dipeptidase en_US
dc.type Thesis en_US
dc.degree.programme Molecular and Cellular Biology en_US
dc.degree.name Master of Science en_US
dc.degree.department Department of Molecular and Cellular Biology en_US
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