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From the Department of Microbiology, School of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania
Abstract
Crude concentrates containing erythrogenic toxin B were prepared from filtrates or supernatants of cultures of three group A streptococci and the partially purified toxins were studied. Toxin B, like toxin A, appeared to be a protein and was not precipitable by protamine. Toxin B, unlike toxin A, was largely destroyed in the presence of trypsin. Toxin B, in contrast to toxin A, did not flocculate with anti-A antitoxin. In agar gel diffusion tests, a specific precipitin reaction of toxin B-anti-B antitoxin was not identified.
Footnotes
1 This work was begun in the laboratories of the Children's Hospital of Pittsburgh with Ethel Verney. The investigation was supported by grants from the National Institutes of Health, the Western Pennsylvania Chapter of the Arthritis and Rheumatism Foundation and the United Fund of Pittsburgh.
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