Cysteine conjugate beta-lyase activities in rat kidney cortex: subcellular localization and relationship to the hepatic enzyme.
Kidney cortex cysteine conjugate beta-lyase enzymes were characterized using S-(2-benzothiazolyl)-L-cysteine and S-(1,2-dichlorovinyl)-L-cysteine as substrates. The contribution of the hepatic form of cysteine conjugate beta-lyase to renal metabolism of these S-cysteine conjugates is not substantial. No cysteine conjugate beta-lyase activity was found in kidney cortex brush border membrane vesicles. Two cysteine conjugate beta-lyase activities with densities corresponding to the mitochondrial and soluble fractions were separated on Percoll gradients.
D000818:Animals; D013437:Carbon-Sulfur Lyases; D003600:Cytosol / Q000201:enzymology; D007672:Kidney Cortex / Q000201:enzymology*; D008099:Liver / Q000201:enzymology*; D008190:Lyases / Q000378:metabolism*; D008297:Male; D008928:Mitochondria / Q000201:enzymology; D009928:Organ Specificity; D051381:Rats; D011919:Rats, Inbred Strains; D012995:Solubility; D013347:Subcellular Fractions / Q000201:enzymology
D008190:Lyases; D013437:Carbon-Sulfur Lyases; C019969:S-alkylcysteine lyase