| Literature DB >> 4928818 |
V A Fischetti, E C Gotschlich, A W Bernheimer.
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.Entities:
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Year: 1971 PMID: 4928818 PMCID: PMC2138921 DOI: 10.1084/jem.133.5.1105
Source DB: PubMed Journal: J Exp Med ISSN: 0022-1007 Impact factor: 14.307