Inhibition of pepsin activity by unconjugated bile acids. Inverse relation to number of hydroxyl groups.
The unconjugated bile acids cholic, deoxycholic, chenodeoxycholic, and lithocholic acid were each found to inhibit pepsin activity in vitro against the refined substrate n-adenosyl-L-phenylalanyl-L-3,5-diiodotyrosine (n-APDT). The degree of inhibition was inversely proportional to the number of hydroxyl substituents on the bile acid molecule. The implications of these findings in relation to the occurrence of peptic ulceration in patients undergoing Roux-Y biliary diversion is discussed.
D000818:Animals; D001647:Bile Acids and Salts / Q000494:pharmacology*; D002635:Chenodeoxycholic Acid / Q000494:pharmacology; D003840:Deoxycholic Acid / Q000494:pharmacology; D004151:Dipeptides / Q000378:metabolism; D008095:Lithocholic Acid / Q000494:pharmacology; D010434:Pepsin A / Q000037:antagonists & inhibitors* / Q000378:metabolism; D013552:Swine
D001647:Bile Acids and Salts; D004151:Dipeptides; C035733:N-adenosyl-phenylalanyl-3,5-diiodotyrosine; D003840:Deoxycholic Acid; D002635:Chenodeoxycholic Acid; D008095:Lithocholic Acid; D010434:Pepsin A