DIGESTION OF THE OXIDIZED B-CHAIN OF INSULIN BY HUMAN NEUTROPHILE PROTEASES - ELASTASE AND CHYMOTRYPSIN-LIKE PROTEASE

被引：12

作者：

LEVY, H

FEINSTEIN, G

机构：

[1] Department of Biochemistry, The George S. Wise Center of Life Sciences, Tel-Aviv University, Tel-Aviv

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 567卷 / 01期

关键词：

Chymotrypsin-like protease; Elastase; Insulin B chain; Protease digestion;

D O I：

10.1016/0005-2744(79)90169-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The specificities of human neutrophile elastase and chymotrypsin-like protease towards oxidized insulin B chain were studied. The neutrophile elastase was found to differ from porcine pancreatic elastase in its specificity towards insulin B chain. The neutrophile elastase preferred mostly valine near the cleaved bond in contrast to pancreatic elastase which preferred alanine as well as valine near the cleaved bond. Human neutrophile chymotrypsin-like protease was found to cleave mostly bonds involving leucine and phenylanine. © 1979.

引用

页码：35 / 42

页数：8

共 16 条

[1]

ATLAS D, 1974, ISRAEL J CHEM, V12, P455

[2] ACTION OF HUMAN LYSOSOMAL ELASTASE ON OXIDIZED-B CHAIN OF INSULIN [J].