title: Evidence that cholic acid CoA ligase is located asymmetrically on the cytoplasmic surface of hepatic microsomal vesicles.
abstract: 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.
mesh_terms: 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
chemical_list: D002793:Cholic Acids; D013656:Taurocholic Acid; D010450:Endopeptidases; D003066:Coenzyme A Ligases; C019890:choloyl-CoA synthetase