McClelland, D.A. and McLaughlin, S.H. and Freedman, R.B. and Price, N.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.
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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 22.214.171.124) 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.
|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:||30 May 2012 10:58|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/19373 (The current URI for this page, for reference purposes)|
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