Purification and characterization of the L component of Streptococcus zymogenes lysin.
By utilizing conventional techniques of pressure ultrafiltration, gel filtration chromatography, diethylaminoethyl cellulose chromatography, and preparative polyacrylamide electrophoresis, the L component of the group D lysin produced by Streptococcus zymogenes strains has been purified to a state of homogeneity as determined by the techniques of disc-gel electrophoresis at pH 9.3 and 4.3 and isoelectric focusing. The L component was found to be a protein possessing a molecular weight of 11,000 with a slight net negative charge at physiological pH.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001322:Autoanalysis; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003470:Culture Media; D004589:Electrophoresis, Disc; D004912:Erythrocytes / Q000276:immunology; D005374:Filtration; D006460:Hemolysin Proteins / Q000032:analysis* / Q000302:isolation & purification; D006461:Hemolysis; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008970:Molecular Weight; D011817:Rabbits; D013291:Streptococcus / Q000032:analysis* / Q000254:growth & development; D013301:Streptolysins / Q000032:analysis / Q000302:isolation & purification
D000596:Amino Acids; D003470:Culture Media; D006460:Hemolysin Proteins; D013301:Streptolysins