TRYPTIC HYDROLYSIS AT ASPARAGINE RESIDUES IN GLOBIN CHAINS

被引：11

作者：

CASEY, R ^{[1
]}

LANG, A ^{[1
]}

机构：

[1] UNIV CAMBRIDGE ADDENBROOKES HOSP, DEPT CLIN BIOCHEM, CAMBRIDGE CB2 2Q5, ENGLAND

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1976年 / 434卷 / 01期

关键词：

D O I：

10.1016/0005-2795(76)90049-0

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：

Commercially available tosyl-phenylmethychloride [Tos-PheCH2C]-treated or untreated bovine trypsin (EC 3.4.21.4) is shown to catalyse minor tryptic hydrolysis at the carboxyl side of asparagine residues in globin chains. This activity is not removed by the purification of enzyme, using CM-cellulose chromatography and subsequent affinity chromatography on trypsin inhibitor columns; neither is it inhibited by Tos-PheCH2Cl treatment of the CM-cellulose purified enzyme. The ability to hydrolyse globin chains at asparagine residues may represent an inherent feature of the trypsin molecule.

引用

页码：184 / 188

页数：5

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