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Journal of Dairy Science Vol. 50 No. 7 1019-1024
© 1967 by American Dairy Science Association ®
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Lactic Streptococcal Phage-Associated Lysin. II. Purification and Characterizaton1

D. R. Tourville and S. Tokuda2

Departments of Agricultural Biochemistry and Medical Microbiology, University of Vermont, Burlington

ABSTRACT

c10-Lysin was purified approximately 1,700-fold by a multistep procedure involving use of the ultracentrifuge, ammonium sulfate fractionation, gel filtration, and ion exchange chromatography. The purified c10-lysin lost activity relatively rapidly at room temperature and when stored at 4 or –60 C. The presence of 2-mercaptoethanol and EDTA preserved but did not increase c10-lysin activity. Both monovalent and divalent cations activated c10-lysin. Low concentrations of p-chloromercuribenzoate completely inhibited c10-lysin activity, while relatively high concentrations of iodoacetamide were required to inhibit c10-lysin activity. The purified c10-lysin has a pH optimum of 6.0-6.5 and is destroyed by mild heat treatment. The Q10 and energy of activation values for c10-lysin are 3.9 and 25 Kcal, respectively. Electrophoretically, c10-lysin migrated toward the cathode at pH 8.6. No proteolytic activity was detected when purified c10-lysin reacted with casein at several pH values. Another lactic streptococcal phage-associated lysin (c2-lysin) was studied. Crude c2-lysin showed physico-chemical characteristics similar to crude and purified c10-lysin preparations; however, the pattern of crude c2- and c10-lysin activity differed.

FOOTNOTES

1 From a portion of a dissertation by the senior author in partial fulfillment of requirements for the Ph.D. degree. Present address: Buffalo General Hospital, Buffalo, New York. Contribution from the University of Vermont, Agricultural Experiment Station, Journal Article no. 183.

2 Present address: Department of Microbiology, University of New Mexico Medical School, Albuquerque, New Mexico.






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Copyright © 1967 by the American Dairy Science Association ®.