Enrichment of Enzyme Activity on Deformylation of 1-NFK-Lysozyme1
- 1 August 1976
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 80 (2) , 409-412
- https://doi.org/10.1093/oxfordjournals.jbchem.a131292
Abstract
The formamide linkage of an inactive lysozyme derivative (1-NFK-lysozyme), formed by selective ozonization of tryptophan 62 in hen egg-white lysozyme [EC 3. 2. 1. 17] was hydrolyzed with dilute acid faster in the frozen state at about −10° than at 20°. On hydrolysis of 1-NFK-lysozyme the low lytic activity increased to approximately 80% of that of native lysozyme. It is suggested that the binding ability associated with kynurenine 62 in the lysozyme derivative formed by this hydrolysis may be responsible for increase in enzymatic activity.This publication has 2 references indexed in Scilit:
- Localization of non-essential tryptophan residues for the biological activity of lysozymetJournal of Molecular Biology, 1967
- The Preparation and Enzymatic Hydrolysis of Reduced and S-Carboxymethylated ProteinsJournal of Biological Chemistry, 1963