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. 1975 Sep;12(3):679–686. doi: 10.1128/iai.12.3.679-686.1975

Guanidine extraction of streptococcal M protein.

H Russell, R R Facklam
PMCID: PMC415339  PMID: 809363

Abstract

A new method of extracting M protein from streptococcal cell walls has been presented. The extracting agent was guanidine-hydrochloride, a protein denaturant. The crude guanidine extract was further purified by ammonium sulfate and pH 5 fractionation and by hydroxyapatite column chromatography. Three major protein peaks were eluted from the hydroxyapatite column with 0.01, 0.1 and 0.3 M phosphate buffer, respectively. Protein fractions eluted at 0.1 and 0.3 M phosphate concentractions contained antigens that precipitated with homologous M-protein specific antisera, whereas the 0.01 M phosphate fraction had no immunological activity. The fraction eluted with 0.3 M phosphate was electrophoretically homogeneous in sodium dodecyl sulfate-acrylamide gels and elicited the production of bactericidal antibodies in rabbits. The 0.1 M phosphate buffer eluant was electrophoretically heterogeneous and did not elicit the production of bactericidal antibodies in rabbits.

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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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