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. 1971 May 1;133(5):1105–1117. doi: 10.1084/jem.133.5.1105

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

Vincent A Fischetti 1, Emil C Gotschlich 1, Alan W Bernheimer 1
PMCID: PMC2138921  PMID: 4928818

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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Selected References

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