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.

PDF 171.pdf - Published Version Restricted to Registered users only Download (1134Kb) | Request a copy

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

Actions (login required)

View Item