Refolding of riboflavin carrier protein as probed by biochemical and immunological parameters

Kuzhandhai Velu, N. ; Karande, Anjali A. ; Adiga, P. Radhakantha (1996) Refolding of riboflavin carrier protein as probed by biochemical and immunological parameters Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, 1293 (2). pp. 231-237. ISSN 0167-4838

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/016748...

Related URL: http://dx.doi.org/10.1016/0167-4838(95)00253-7

Abstract

The unfolding of the chicken egg white riboflavin carrier protein by disulfide reduction with dithiothreitol led to aggregation with concomitant loss of ligand binding characteristics and the capacity to interact with six monoclonal antibodies directed against surface-exposed discontinuous epitopes. The reduced protein could, however, bind to a monoclonal antibody recognizing sequential epitope. Under optimal conditions of protein refolding, the vitamin carrier protein regained its folded structure with high efficiency with simultaneous complete restoration of hydrophobic flavin binding site as well as the epitopic conformations exposed at the surface in a manner comparable to its native form.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Disulfide Reduction; Epitope; Ligand Binding; Monoclonal Antibody; Refolding; Riboflavin Carrier Protein
ID Code:26813
Deposited On:08 Dec 2010 13:08
Last Modified:13 May 2011 04:14

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