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Modification of tryptophan residues of lysozyme with o-benzoquinone and physicochemical studies on the modified enzyme

Narasimhan, S and Vithayathil, PJ (1987) Modification of tryptophan residues of lysozyme with o-benzoquinone and physicochemical studies on the modified enzyme. In: Indian Journal of Biochemistry & Biophysics, 24 (3). pp. 146-152.

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Abstract

To study the effect of the reaction of o-benzoquinone with lysozyme on the activity and the conformational changes brought about in the enzyme mol. as a result of the modification of its tryptophan residues, the o-benzoquinone deriv. of lysozyme was prepd. by carrying out the reaction in acidic medium and purified chromatog. Amino acid anal. difference spectral calculations showed that on an av., 3 out of the 6 tryptophan residues in lysozyme, underwent chem. modification. The ionization characteristics of modified tryptophan residues of lysozyme were similar to that of o-benzoquinone derivative of N-acetyl-DL-tryptophan. Fluorescence and CD spectral studies of the modified lysozyme clearly indicated the change in conformation of the modified deriv. as compared to that of the native enzyme

Item Type: Journal Article
Additional Information: Copyright of this article belongs to National Institute of Science Communication and Information Resources
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 12 Jun 2008
Last Modified: 27 Aug 2008 13:26
URI: http://eprints.iisc.ernet.in/id/eprint/14275

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