COMPARISON OF THE ACTIVITIES OF PROTEIN DISULFIDE-ISOMERASE AND THIOREDOXIN IN CATALYZING DISULFIDE ISOMERIZATION IN A PROTEIN SUBSTRATE

被引：114

作者：

HAWKINS, HC ^{[1
]}

BLACKBURN, EC ^{[1
]}

FREEDMAN, RB ^{[1
]}

机构：

[1] UNIV KENT,BIOL LAB,CANTERBURY CT2 7NJ,KENT,ENGLAND

来源：

BIOCHEMICAL JOURNAL | 1991年 / 275卷

关键词：

D O I：

10.1042/bj2750349

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：

1. The activities of protein disulphide-isomerase (PDI) and thioredoxin in catalysing disulphide bond isomerization in a protein substrate were compared by using the standard assay, namely the re-activation of 'scrambled' RNAase. 2. The specific activity of PDI was 25-fold greater than that of thioredoxin. 3. The greater efficiency of PDI compared with thioredoxin is considered to be due more to the presence of multiple catalytic domains in PDI than to differences in their active-site sequences. 4. Data and procedures were defined for expressing enzyme activity in standard units, i.e. mu-mol of active RNAase generated/min.

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页码：349 / 353

页数：5

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