The denaturation of β-lactoglobulin-A at pH 2

Ananthanarayanan, VS and Ahmad, F and Bigelow, CC (1977) The denaturation of β-lactoglobulin-A at pH 2. In: Biochimica et Biophysica Acta (BBA) - Protein Structure, 492 (1). pp. 194-203.

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Abstract

The denaturation of β-lactoglobulin-A by heat and guanidine hydrochloride at pH 2 has been investigated. The effect of ethylene glycol on the thermal denaturation at this pH has also been studied. The conditions of the experiments have been chosen so as to eliminate complications arising out of disulfide interchange, changes in the degree of association of the protein during denaturation, and intermolecular aggregation. The physical parameters characterizing the denatured states of the protein which are produced by heat and guanidine hydrochloride have been determined. The thermodynamic parameters for these transitions have been estimated using a two-state hypothesis in each case. Both the physical and thermodynamic parameters indicate that the heat-denatured state of β-lactoglobulin-A retains about 15-20% of residual structure which is destroyed on adding guanidine hydrochloride.

Item Type:	Journal Article
Publication:	Biochimica et Biophysica Acta (BBA) - Protein Structure
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	04 Feb 2010 06:11
Last Modified:	19 Sep 2010 05:50
URI:	http://eprints.iisc.ac.in/id/eprint/24496

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