Wang C S
Lipoprotein and Atherosclerosis Research Program, College of Medicine, University of Oklahoma, Oklahoma City.
Biochem Biophys Res Commun. 1988 Sep 15;155(2):950-5. doi: 10.1016/s0006-291x(88)80588-6.
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.
已开发出一种从人胰腺中纯化羧基酯脂肪酶的方法。纯化后的酶经测定的N端10个氨基酸残基为NH2-Ala-Lys-Leu-Gly-Ala-Val-Tyr-Thr-Glu-Gly，与母乳胆汁盐激活脂肪酶的末端相同。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定，人胰腺羧基酯脂肪酶的表观分子量略小于母乳胆汁盐激活脂肪酶（分别为105,000和125,000）。因此，人胰腺羧基酯脂肪酶和母乳胆汁盐激活脂肪酶有可能是由同一基因通过不同的剪接或翻译后修饰产生的。或者，它们也可能只是两个密切相关但独立的基因的产物。
