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J Virol. 1967 August; 1(4): 701-710
Copyright © 1967 American Society for Microbiology. All Rights Reserved.

Characteristics of a Lytic Enzyme Induced by Bacteriophage Infection of Micrococcus lysodeikticus1

J. M. Goepfert2 and H. B. Naylor

a Department of Microbiology, Division of Biological Sciences, Cornell University, Ithaca, New York

ABSTRACT

A lytic enzyme induced in Micrococcus lysodeikticus strain 1 by infection with N1 bacteriophage was purified 45- to 50-fold by ammonium sulfate precipitation, acid precipitation, and selective adsorption of contaminating proteins with calcium phosphate gel. The optimal pH for activity of the enzyme was 6.5 to 7.0. Maximal activity occurred at 45 to 50 C and at an ionic strength of 0.06. The enzyme had a limited specificity and lysed cell walls of M. lysodeikticus with the release of dinitrofluorobenzene reactive groups. Living cells were lysed in the absence of phage; however, the rate of lysis increased when phage was present in excess of 10 particles per bacterial cell. Young cells were most sensitive, and the sensitivity decreased to a minimum with stationary-phase cells. Acting synergistically, lysozyme and the N1-induced lysin caused lysis of cells which were resistant to either enzyme acting independently. The N1 lysin did not exhibit proteolytic activity.

FOOTNOTES

2 Present address: Food Research Institute, University of Wisconsin, Madison 53706.

1 Submitted by the senior author in partial fulfillment of the requirements for the Ph.D. degree.

J Virol. 1967 August; 1(4): 701-710
Copyright © 1967 American Society for Microbiology. All Rights Reserved.





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