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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1989-6-2
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pubmed:abstractText |
Cysteine conjugate beta-lyase (beta-lyase) was purified to electrophoretic homogeneity from the kidney cytosol of male Wistar rats. The highly purified enzyme exhibited a monomeric molecular weight of 50,000 Da and was active in the alpha-beta elimination of cysteine conjugates including S-(1,2-dichlorovinyl)-L-cysteine (DCVC), S-(1,1,2,2-tetrafluoroethyl)-L-cysteine (TFEC), and S-(2-benzothiazolyl)-L-cysteine, particularly toward DCVC and TFEC. The purified enzyme also exhibited glutamine transaminase K activity with phenylalanine and alpha-keto-gamma-methiolbutyrate as substrates. An antibody was raised to the purified rat protein in sheep and the crude immune serum affinity purified, yielding a specific antibody that recognized only the beta-lyase protein in whole kidney homogenates. Immunocytochemical studies on rat kidney sections stained with the purified antibody revealed that the cytosolic beta-lyase enzyme was mainly localized in the pars recta of the proximal tubule in untreated rats. This localization is coincident with the site-specific kidney necrosis produced by hexachloro-1,3-butadiene (HCBD). These results indicate that the tissue localization of beta-lyase in the proximal tubule plays an important role in determining the specific nephrotoxicity produced by halogenated alkenes such as HCBD.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Butadienes,
http://linkedlifedata.com/resource/pubmed/chemical/Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Transaminases,
http://linkedlifedata.com/resource/pubmed/chemical/glutamine - phenylpyruvate...,
http://linkedlifedata.com/resource/pubmed/chemical/hexachlorobutadiene,
http://linkedlifedata.com/resource/pubmed/chemical/kynurenine-oxoglutarate transaminase
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0041-008X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
98
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
185-97
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2711386-Animals,
pubmed-meshheading:2711386-Antibody Specificity,
pubmed-meshheading:2711386-Butadienes,
pubmed-meshheading:2711386-Cross Reactions,
pubmed-meshheading:2711386-Cytosol,
pubmed-meshheading:2711386-Immunohistochemistry,
pubmed-meshheading:2711386-Kidney,
pubmed-meshheading:2711386-Lyases,
pubmed-meshheading:2711386-Male,
pubmed-meshheading:2711386-Molecular Weight,
pubmed-meshheading:2711386-Rats,
pubmed-meshheading:2711386-Rats, Inbred Strains,
pubmed-meshheading:2711386-Transaminases
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pubmed:year |
1989
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pubmed:articleTitle |
Cysteine conjugate beta-lyase of rat kidney cytosol: characterization, immunocytochemical localization, and correlation with hexachlorobutadiene nephrotoxicity.
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pubmed:affiliation |
University of Surrey, Biochemistry Department, Guildford, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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