Kinetic Studies on the Chemical Modification of Lysozyme by N-Bromosuccinimide and Its Protection by Substrates and Analogs1
- 1 June 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 81 (6) , 1583-1586
- https://doi.org/10.1093/oxfordjournals.jbchem.a131616
Abstract
The chemical modification of tryptophan residues of hen egg-white lysozyme by N-bromosuccinimide (NBS) was studied kinetically by the stopped-flow method, monitoring changes in absorbance and fluorescence. One most rapidly reacting tryptophan residue, probably Trp 62, was clearly distinguished from four other residues in terms of rate of modification. This residue was protected by ethylene glycol chitin, N-acetyl glucosamine (NAG), and tn-NAG, but not by gluconolactone. The dissociation constant Kd of the enzyme-ligand complex was obtained from the protection effects. These results are in good agreement with results previously obtained.This publication has 2 references indexed in Scilit:
- Some relations between structure and function in hemoglobinJournal of Molecular Biology, 1963
- A Method for Characterizing the Type and Numbers of Groups Involved in Enzyme ActionJournal of Biological Chemistry, 1961