McClelland, D.A., McLaughlin, Stephen H., Freedman, Robert B., Price, Nicholas C. (1995) The refolding of hen egg white riboflavin-binding protein: effect of protein disulphide isomerase on the reoxidation of the reduced protein. Biochemical Journal, 311 . pp. 133-137. ISSN 0264-6021. (doi:10.1042/bj3110133) (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:19373)
| 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. | |
| Official URL: https://doi.org/10.1042/bj3110133 |
Abstract
Hen egg white riboflavin-binding protein (RfBP) contains nine disulphide bonds. Provided these remain intact, the refolding of RfBP after incubation in 6 M guanidinium chloride is highly efficient with at least 95 % of the binding activity regained within 3 min. Kinetic studies indicate that this regain consists of at least two phases. When the disulphide bonds of RfBP are reduced, reoxidation using a mixture of oxidized and reduced glutathione leads to less than 5 % recovery of activity. However, if protein disulphide isomerase (PDI; EC 5.3.4.1) is present during the reoxidation nearly 50 % activity can be regained, suggesting that PDI may play an important role in the maturation of RfBP in vivo.
| Item Type: | Article |
|---|---|
| DOI/Identification number: | 10.1042/bj3110133 |
| Subjects: |
Q Science > QP Physiology (Living systems) > QP517 Biochemistry Q Science > QP Physiology (Living systems) > QP506 Molecular biology |
| Divisions: | Divisions > Division of Natural Sciences > Biosciences |
| Depositing User: | O.O. Odanye |
| Date Deposited: | 04 Jun 2009 10:30 UTC |
| Last Modified: | 09 Mar 2023 11:31 UTC |
| Resource URI: | https://kar.kent.ac.uk/id/eprint/19373 (The current URI for this page, for reference purposes) |
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