An activity of hydrolyzing elastase substrate succinyltrialanine p-nitroanilide in human bile.
Human hepatic bile contained an activity of hydrolyzing N-succinyl-L-alanyl-Lalanyl-L-alanine-p-nitroanilide, a substrate for elastase. The activity was associated with high molecular weight materials and was metal dependent. Neither elastase nor elastase-alpha 2-macroglobulin complex was implicated in this activity.
D000813:Anilides; D000818:Animals; D001646:Bile / Q000378:metabolism*; D002417:Cattle; D002850:Chromatography, Gel; D004492:Edetic Acid / Q000494:pharmacology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D009842:Oligopeptides; D010196:Pancreatic Elastase; D012694:Serine / Q000037:antagonists & inhibitors; D000511:alpha-Macroglobulins / Q000276:immunology
D000813:Anilides; D009842:Oligopeptides; D000511:alpha-Macroglobulins; D012694:Serine; D004492:Edetic Acid; D010196:Pancreatic Elastase