Hawkins, Hilary C., Blackburn, Edith, Freedman, Robert B. (1991) Comparison of the activities of protein disulfide-isomerase and thioredoxin in catalyzing disulfide isomerization in a protein substrate. Biochemical Journal, 275 (2). pp. 349-353. ISSN 0264-6021. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:22970)
| The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. |
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. mu-mol of active RNAase generated/min.
| Item Type: | Article |
|---|---|
| Subjects: | Q Science > QP Physiology (Living systems) |
| Divisions: | Divisions > Division of Natural Sciences > Biosciences |
| Depositing User: | O.O. Odanye |
| Date Deposited: | 04 Nov 2009 11:11 UTC |
| Last Modified: | 05 Nov 2024 10:02 UTC |
| Resource URI: | https://kar.kent.ac.uk/id/eprint/22970 (The current URI for this page, for reference purposes) |
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