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Association-Dissociation Behavior of Sesame alpha-Globulin in Electrolyte Solutions

Prakash, V. and Nandi, P. K. (1977) Association-Dissociation Behavior of Sesame alpha-Globulin in Electrolyte Solutions. Journal of Biological Chemistry, 252 (1). pp. 240-243.

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Abstract

The major protein fraction, alpha-globulin, of sesame seed CS’esamum indicum L.) contains subunits which are associated predominantly by hydrophobic interactions. Effects of various salts show the following effectiveness of anions in dissociating the proteins, SO,*- < Cl- < Br- < C104- < SCN- 4 I- < CCl,COO-, the first two members being association-inducing ions. CC1,COONa is found to be the most effective among the series in causing dissociation. The cations Lit, Na+, K+, and Cs+ induce association, the order of effectiveness being Cs+ - K+ > Na+ > IA+. The low concentration of salts (anions) necessary to induce dissociation does not involve a detectable change in protein conforma- tion. The discrepancy between the effectiveness of the anions in dissociating the protein and the Hofmeister pattern of these ions has been discussed.

Item Type: Article
Uncontrolled Keywords: sesame seed alpha-Globulin electrolyte solutions Association-Dissociation Behavior
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry
600 Technology > 08 Food technology > 22 Legumes-Pulses
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 08 Jan 2008 10:20
Last Modified: 28 Dec 2011 09:32
URI: http://ir.cftri.com/id/eprint/1612

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