REMARKABLE HOMOLOGY ABOUT DISULFIDE BRIDGES OF A TRYPSIN-LIKE ENZYME FROM STREPTOMYCES GRISEUS

被引：49

作者：

JURASEK, L

FACKRE, D

SMILLIE, LB

机构：

[1] Department of Biochemistry, University of Alberta, Edmonton

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1969年 / 37卷 / 01期

基金：

英国医学研究理事会;

关键词：

BAEE; benzoyl-l-arginine ethyl ester;

D O I：

10.1016/0006-291X(69)90885-7

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：

A trypsin-like enzyme which cleaves only the arginine and lysine peptide bonds of the oxidized chains of insulin has been isolated from commercial preparations of pronase. Amino acid analyses revealed the presence of only one histidine and six half-cystine residues. Determination of the amino acid sequences about the three disulfide bridges has demonstrated remarkable homology with three corresponding bridges in bovine pancreatic trypsin. These sequences include both the active serine and histidine as well as the cationic specificity site for trypsin substrates. © 1969.

引用

页码：99 / &

共 20 条

[1] LOCATION OF DISULPHIDE BRIDGES BY DIAGONAL PAPER ELECTROPHORESIS - DISULPHIDE BRIDGES OF BOVINE CHYMOTRYPSINOGEN A [J].