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  • Title: Isolations of protein A and protein G from the bacterial surface.
    Author: Sting R, Lauerman L, Blobel H.
    Journal: Zentralbl Bakteriol; 1990 Aug; 273(3):306-12. PubMed ID: 2206199.
    Abstract:
    Ten tested cultures each of Staphylococcus aureus (S. aureus) and of Streptococcus belonging to serological group G bound human IgG to a high extent. Protein A could be solubilized from strain Cowan I of S. aureus by lysozyme, mutanolysine, hydroxylammoniumchloride, hot acid extraction or lysostaphin and subsequently purified by affinity chromatography on human IgG-sepharose. The purified protein A preparation had molecular weights between 29,000 and 63,000 D and inhibited binding of 125I-labeled human IgG to S. aureus Cowan I. Protein G could be solubilized from strain 26540 of the G-streptococci with lysozyme or hot acid extraction and purified by affinity chromatography on human IgG-sepharose. The purified protein G revealed a molecular weight of 67,000 D and inhibited binding of human IgG to the G-streptococci.
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