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Studies on tryptophan residues of Abrus agglutinin Stopped-flow kinetics of modification and fluorescence-quenching studies

Patanjali, SR and Swamy, MJ and Surolia, Avadhesha (1987) Studies on tryptophan residues of Abrus agglutinin Stopped-flow kinetics of modification and fluorescence-quenching studies. In: Biochemical Journal, 243 (1). pp. 79-86.

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Abstract

The presence of two essential tryptophan residues/molecule was implicated in the binding site of Abrus agglutinin [Patanjali, Swamy, Anantharam, Khan & Surolia (1984) Biochem. J. 217, 773-781]. A detailed study of the stopped-flow kinetics of the oxidation of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues into two phases was observed upon ligand binding. The heterogeneity of tryptophan exposure was substantiated by quenching studies with acrylamide, succinimide and Cs+. Our study revealed the microenvironment of tryptophan residues to be hydrophobic, and also the presence of acidic amino acid residues in the vicinity of surface-localized tryptophan residues.

Item Type: Journal Article
Additional Information: Copy right of this article belongs to Portland Press.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 15 Jan 2010 06:44
Last Modified: 19 Sep 2010 05:37
URI: http://eprints.iisc.ernet.in/id/eprint/21417

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