PURIFICATION AND PHYSICAL PROPERTIES OF GROUP C STREPTOCOCCAL PHAGE-ASSOCIATED LYSIN

doi:10.1084/jem.133.5.1105

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PURIFICATION AND PHYSICAL PROPERTIES OF GROUP C STREPTOCOCCAL PHAGE-ASSOCIATED LYSIN

Vincent A. Fischetti Ph.D.¹, Emil C. Gotschlich M.D.¹, and Alan W. Bernheimer Ph.D.¹

¹ From the Department of Microbiology, New York University School of Medicine, New York 10016, and The Rockefeller University, New York 10021

A purification procedure for the Group C phage-associated lysinis described utilizing tetrathionate to protect the enzyme's-SH group(s) from thiol-inactivating agents. A 652-fold purificationhas been accomplished yielding a solution in which the enzymeactivity corresponds to essentially a single band on polyacrylamidegel which accounts for 70% of the total protein in the preparation.A molecular weight of 101,000 and frictional ratio of 1.526was determined for the lysin utilizing experimentally determinedvalues for its Stokes radius and sedimentation coefficient.

Submitted on January 14, 1971

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