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J. Biochem, 1976, Vol. 80, No. 2 409-412
© 1976 Japanese Biochemical Society

other

Enrichment of Enzyme Activity on Deformylation of 1-NFK-Lysozyme1

Nobuyuki YAMASAKI*, Takahiro TSUJITA*, Fumio SAKIYAMA** and Kozo NARITA**

*Laboratory of Biochemistry, Faculty of Agriculture, Ehime University Matsuyama, Ehime 790
**Division of Protein Chemistry, Institute for Protein Research, Osaka University Suita, Osaka 565

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.

1 This work was supported by a grant from the Ministry of Education, Science and Culture, of Japan.


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