Regulation of protein binding from 35S-(pentachlorobutadienyl)-L-cysteine in renal epithelial cells and mitochondria.
The protein binding rate of the reactive metabolite formed from the beta-lyase-mediated cleavage of S-(1,2,3,4-pentachloro-1,3-butadienyl)-L-cysteine was determined in rat kidney fractions and isolated renal epithelial cells. The binding was highest in mitochondria and localized to the outer membrane/intermembrane space and matrix. The matrix activity was stimulated by an alpha-keto acid. Soluble thiols and anoxia inhibited the protein binding.
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Dept of Forensic Medicine, Karolinska Institute, Stockholm, Sweden.
D000818:Animals; D001711:Biotransformation; D002070:Butadienes / Q000378:metabolism* / Q000633:toxicity; D003545:Cysteine / Q000031:analogs & derivatives* / Q000378:metabolism / Q000633:toxicity; D004847:Epithelial Cells; D004848:Epithelium / Q000378:metabolism; D066298:In Vitro Techniques; D007672:Kidney Cortex / Q000166:cytology / Q000378:metabolism*; D008297:Male; D008928:Mitochondria / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D011919:Rats, Inbred Strains; D013347:Subcellular Fractions / Q000378:metabolism; D013462:Sulfur Radioisotopes
D002070:Butadienes; D013462:Sulfur Radioisotopes; C039330:S-pentachlorobuta-1,3-dien-yl-cysteine; D003545:Cysteine