Abstract
By utilizing conventional techniques of pressure ultrafiltration, gel filtration chromatography, diethylaminoethyl cellulose chromatography, and preparative polyacrylamide electrophoresis, the A component of the group D lysin produced by Streptococcus zymogenes has been purified to a state of apparent homogeneity when determined by the techniques of anionic and cationic disc gel electrophoresis. The A component was found to be a protein possessing a molecular weight of 27,000, a sedimentation coefficient approximating 3.2S, and a net negative charge at physiological pH.
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