Studies on human pancreatic lipase

Samples of pancreatic juice derived from drainage fluid of patients undergoing pancreatic surgery have been fractionated by gel filtration yielding up to three components showing lipolytic activity against emulsified triglyceride. The “fast” (high molecular weight) lipase fraction has been further studied and has been found to be stable for several months in solution in 1.0% gum acacia in 0.14 M sodium chloride. This fraction has no dialysable co-factor and its activity is not potentiated by sodium deoxycholate or calcium ions at pH 8.5. It is strongly inhibited by human serum and by human and bovine serum albumin. The degree of inhibition by albumin depends on the order in which the enzyme and albumin are added to the substrate. The inhibition by albumin is reversed by deoxycholate.