Purification and physical properties of group C streptococcal phage-associated lysin.
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.
D000179:Acrylates; D001426:Bacterial Proteins / Q000032:analysis; D001431:Bacteriological Techniques; D001435:Bacteriophages; D002845:Chromatography; D003720:Densitometry; D004586:Electrophoresis; D004789:Enzyme Activation; D005782:Gels; D008239:Lysine / Q000032:analysis / Q000302:isolation & purification*; D008242:Lysogeny; D008970:Molecular Weight; D013053:Spectrophotometry; D013291:Streptococcus / Q000201:enzymology*; D013885:Thiosulfates / Q000494:pharmacology
D000179:Acrylates; D001426:Bacterial Proteins; D005782:Gels; D013885:Thiosulfates; D008239:Lysine