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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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 |
|---|---|
| Publication: | Indian Journal of Biochemistry & Biophysics |
| Publisher: | National Institute of Science Communication and Information Resources |
| 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.ac.in/id/eprint/14275 |
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