The refolding of hen egg white riboflavin-binding protein: effect of protein disulphide isomerase on the reoxidation of the reduced protein.

McClelland, D.A. and McLaughlin, Stephen H. and Freedman, Robert B. and 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. (The full text of this publication is not available from this repository)

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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
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: O.O. Odanye
Date Deposited: 04 Jun 2009 10:30
Last Modified: 16 Jun 2014 14:08
Resource URI: http://kar.kent.ac.uk/id/eprint/19373 (The current URI for this page, for reference purposes)
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