Purification of carboxyl ester lipase from human pancreas and the amino acid sequence of the N-terminal region.
A procedure for the purification of carboxyl ester lipase from human pancreas has been developed. The determined N-terminal 10 amino acid residues of the purified enzyme, NH2-Ala-Lys-Leu-Gly-Ala-Val-Tyr-Thr-Glu-Gly, was identical to the terminal of human milk bile salt-activated lipase. The human pancreatic carboxyl ester lipase has an apparent molecular weight slightly smaller than that of human milk bile salt-activated lipase (105,000 vs 125,000) as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Thus, it is possible that the human pancreatic carboxyl ester lipase and human milk bile salt-activated lipase could be produced by the same gene by a different splice or post-translational modification. Alternatively, they could simply be the products of two closely related but separate genes.
Lipoprotein and Atherosclerosis Research Program, College of Medicine, University of Oklahoma, Oklahoma City.
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Wang
D000595:Amino Acid Sequence; D043182:Carboxylesterase; D002265:Carboxylic Ester Hydrolases / Q000302:isolation & purification*; D006801:Humans; D008895:Milk, Human / Q000201:enzymology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D013379:Substrate Specificity
D002265:Carboxylic Ester Hydrolases; D043182:Carboxylesterase