Evidence that cholic acid CoA ligase is located asymmetrically on the cytoplasmic surface of hepatic microsomal vesicles.
The cholic acid CoA ligase activity of rat liver was quantitatively inactivated by proteolysis with pronase, chymotrypsin, subtilisin, or proteinase K in intact microsomal vesicles. Under the conditions employed, less than 14% of the lumenal mannose-6-phosphate phosphatase activity was lost, and the mannose-6-phosphate phosphatase activity remained highly latent. After microsomal integrity was disrupted with sodium deoxycholate, protease treatment resulted in a loss of greater than 74% of the mannose-6-phosphate phosphatase activity. Cholic acid CoA ligase activity was unaffected by preincubation of microsomes with sodium taurocholate under conditions that led to the complete expression of latent mannose-6-phosphate phosphatase activity. The data suggest that cholic acid CoA ligase activity is located on the cytoplasmic surface of hepatic microsomal vesicles.
D000818:Animals; D002793:Cholic Acids; D003066:Coenzyme A Ligases / Q000378:metabolism*; D010450:Endopeptidases; D005260:Female; D007425:Intracellular Membranes / Q000201:enzymology*; D008862:Microsomes, Liver / Q000201:enzymology*; D051381:Rats; D013656:Taurocholic Acid / Q000494:pharmacology
D002793:Cholic Acids; D013656:Taurocholic Acid; D010450:Endopeptidases; D003066:Coenzyme A Ligases; C019890:choloyl-CoA synthetase