A stoichiometric analysis of bovine serum albumin-gossypol interactions: a fluorescence quenching study.

Rao, A. G. A. (1992) A stoichiometric analysis of bovine serum albumin-gossypol interactions: a fluorescence quenching study. Indian Journal of Biochemistry & Biophysics, 29 (2). pp. 179-82. ISSN 0301-1208

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Abstract

The interaction of gossypol with bovine serum albumin, human serum albumin and n-bromosuccinimide-modified bovine serum albumin has been followed by fluorescence quenching measurements. The presence of a high affinity site (association constant K = 2.2 x 10(6) M-1) for gossypol on bovine serum albumin and human serum albumin is indicated. The stoichiometry of binding for the high affinity site was evaluated using Job's method of continuous variation, thereby suggesting the formation of 1:1 complex. Modification of the tryptophan residues on bovine serum albumin does not affect the binding of gossypol to either high or low affinity site of albumin.

Item Type:	Article
Uncontrolled Keywords:	bovine serum, albumin gossypol, fluoroscence quenching
Subjects:	600 Technology > 08 Food technology > 19 Lipids-oils/fats > 01 Oilseeds
Divisions:	Protein Chemistry and Technology
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	15 Nov 2021 04:45
Last Modified:	15 Nov 2021 04:45
URI:	http://ir.cftri.res.in/id/eprint/2316

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