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PMID: 2025222 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate.

The Biochemical journal ·Vol. 275 ( Pt 2) ·1991-04-15 ·Pages 349-53

Hawkins HC, Blackburn EC, Freedman RB

Abstract

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. mumol of active RNAase generated/min.

MeSH Terms
Amino Acid Sequence Animals Binding Sites Cattle Disulfides/metabolism Escherichia coli/metabolism Isomerases/metabolism Isomerism Kinetics Liver/enzymology Molecular Sequence Data Protein Disulfide-Isomerases Ribonucleases/metabolism Thioredoxins/metabolism
Chemicals
Disulfides Thioredoxins Ribonucleases Isomerases Protein Disulfide-Isomerases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hawkins H C
Biological Laboratory, University of Kent, Canterbury, UK.
Blackburn E C
Freedman R B
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2750349
Published
1991-04-15
Pages
349-53
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1150059
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2750349 PMC Full Text View journal details
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