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. 1971 May 1;133(5):1105-17.
doi: 10.1084/jem.133.5.1105.

Purification and physical properties of group C streptococcal phage-associated lysin

V A Fischetti, E C Gotschlich, A W Bernheimer

Purification and physical properties of group C streptococcal phage-associated lysin

V A Fischetti et al. J Exp Med. .

Abstract

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

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