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. 1977 Jun;16(3):867–875. doi: 10.1128/iai.16.3.867-875.1977

Purification and characterization of group A streptococcal T-1 antigen.

R H Johnson, K L Vosti
PMCID: PMC421043  PMID: 70408

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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