Purification and characterization of group A streptococcal T-1 antigen.
A method is described for the recovery of purified T-antigen from crude trypsin extracts of an avirulent strain of M-1 protein deficient, T-type 1 group A Streptococcus. The purified T-antigen was resistant to enzymatic degradation with trypsin and pepsin, formed a single precipitin line with standard T-1 antiserum, failed to react with antisera for teichoic acid, group A carbohydrate, and cross-reactive protein antigens, stimulated only a single precipitin system when rabbits were immunized, contained glycine, aspartic acid, glutamic acid, lysine, and serine as the five most predominant amino acids, and consisted of subunit size isomers.
D000372:Agglutination Tests; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000907:Antibodies, Bacterial / Q000096:biosynthesis; D000942:Antigens, Bacterial / Q000032:analysis / Q000302:isolation & purification; D002241:Carbohydrates / Q000032:analysis; D000939:Epitopes; D011817:Rabbits; D013297:Streptococcus pyogenes / Q000276:immunology*; D013682:Teichoic Acids / Q000032:analysis
D000596:Amino Acids; D000907:Antibodies, Bacterial; D000942:Antigens, Bacterial; D002241:Carbohydrates; D000939:Epitopes; D013682:Teichoic Acids