Velu, Kuzhandhai N and Karande, Anjali A and Adiga, Radhakantha P (1996) Refolding of riboflavin carrier protein as probed by biochemical and immunological parameters. In: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1293 (2). pp. 231-237.
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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:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier Science.|
|Keywords:||Disulfide reduction;Epitope;Ligand binding;Monoclonal antibody;Refolding;Riboflavin carrier protein|
|Department/Centre:||Division of Biological Sciences > Biochemistry
Division of Biological Sciences > Molecular Reproduction, Development & Genetics (formed by the merger of DBGL and CRBME)
|Date Deposited:||10 May 2011 09:12|
|Last Modified:||02 Nov 2011 08:21|
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