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. 1977 May;16(2):673–679. doi: 10.1128/iai.16.2.673-679.1977

Purification and characterization of group A streptococcal pyrogenic exotoxin type C.

P M Schlievert, K M Bettin, D W Watson
PMCID: PMC421008  PMID: 324918

Abstract

Group A streptococcal pyrogenic exotoxin (SPE) type C was partially purified by differential solubility in ethanol and acetate-buffered saline. Toxin prepared in this way consisted of protein and hyaluronic acid. After removal of hyaluronic acid, the toxin remained pyrogenic, enhanced susceptibility of rabbits to letahl endotoxin shock, was stable when treated with acid, base, or pepsin, but was inactivated by heat. Toxin further purified by thin-layer isoelectric focusing was pyrogenic and enhanced the susceptibility of rabbits to lethal endotoxin shock. Purified type C toxin appeared homogeneous when tested by Ouchterlony immunodiffusion and migrated as a single protein band in isoelectric focusing polyacrylamide gels (isoelectric point, 6.7) and sodium dodecyl sulfate-polyacrylamide gels (molecular weight, 13,200). The purified toxin was antigenically distinct from A and B SPE, and antisera raised against the purified toxin neutralized pyrogenic activity. The amino acid composition was determined.

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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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