Inhibition of pepsin activity by ursodeoxycholic acids and chenodeoxycholic acids.
The bile salts of ursodeoxycholic acid, glycoursodeoxycholic acid, tauroursodeoxycholic acid, chenodeoxycholic acid, glycochenodeoxycholic acid, and taurochenodeoxycholic acid were each found to inhibit pepsin proteolytic activity in vitro at various concentrations against the refined substrate n-APDT. The sodium salt of ursodeoxycholic acid was the most potent pepsin inhibitor among those tested.
D000818:Animals; D002635:Chenodeoxycholic Acid / Q000494:pharmacology*; D003840:Deoxycholic Acid / Q000031:analogs & derivatives*; D004151:Dipeptides / Q000037:antagonists & inhibitors; D005999:Glycochenodeoxycholic Acid / Q000494:pharmacology; D066298:In Vitro Techniques; D010434:Pepsin A / Q000037:antagonists & inhibitors*; D013379:Substrate Specificity; D013552:Swine; D013655:Taurochenodeoxycholic Acid / Q000494:pharmacology; D014580:Ursodeoxycholic Acid / Q000031:analogs & derivatives / Q000494:pharmacology*
D004151:Dipeptides; D003840:Deoxycholic Acid; D002635:Chenodeoxycholic Acid; C004980:N-acetylphenylalanyl-3,5-diiodotyrosine; D013655:Taurochenodeoxycholic Acid; C031655:ursodoxicoltaurine; D005999:Glycochenodeoxycholic Acid; C024033:glycoursodeoxycholic acid; D014580:Ursodeoxycholic Acid; D010434:Pepsin A