Abstract
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.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
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