两种人胰凝乳蛋白酶原。纯化与特性鉴定。

The two human chymotrypsinogens. Purification and characterization.

作者信息

De Caro A, Figarella C, Guy O

出版信息

Biochim Biophys Acta. 1975 Feb 27;379(2):431-43. doi: 10.1016/0005-2795(75)90150-6.

Abstract

The two chymotrypsinogens present in human pancreatic juice have been purified and characterized. The zymogens are two immunologically and electrophoretically different proteins. Chymotrypsinogen A, the major chymotryptic component (90% of the total potential N-acetyl-L-tyrosine ethylester activity) is stable in acidic medium. By its molecular weight (approx. 24 000), specific activity (530) and amino acid composition, human chymotrypsinogen A resembles chymotrypsinogens A and B form bovine and porcine pancreas. Chymotrypsinogen B is a minor chymotryptic component (7% of the total potential N-acetyl-L-tyrosine ethylester activity) unstable in acidic medium with a molecular weight slightly higher (approx. 27 000) and a specific activity slightly lower (300) than chymotrypsinogen A. The last 3% of the total potential N-acetyl-L-tyrosine ethylester activity corresponds to a proelastase that we have partially characterized.

摘要

人胰液中存在的两种胰凝乳蛋白酶原已被纯化并进行了特性鉴定。这些酶原是两种在免疫学和电泳方面都不同的蛋白质。胰凝乳蛋白酶原A是主要的胰凝乳蛋白酶成分（占总潜在N - 乙酰 - L - 酪氨酸乙酯活性的90%），在酸性介质中稳定。根据其分子量（约24000）、比活性（530）和氨基酸组成，人胰凝乳蛋白酶原A类似于牛和猪胰腺中的胰凝乳蛋白酶原A和B。胰凝乳蛋白酶原B是次要的胰凝乳蛋白酶成分（占总潜在N - 乙酰 - L - 酪氨酸乙酯活性的7%），在酸性介质中不稳定，分子量略高（约27000），比活性略低于胰凝乳蛋白酶原A（300）。总潜在N - 乙酰 - L - 酪氨酸乙酯活性的最后3%对应于一种我们已部分鉴定的前弹性蛋白酶。