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- W1997161821 abstract "Three different enzymatic extraction procedures were tested for their effectivity in releasing IgG-binding peptides from the streptococcal cell wall. Streptococcus equisimilis strain 12628 isolated from pig was incubated with phage-associated lysin, trypsin and Streptomyces globisporus lytic enzyme and the extracts were investigated by Western blotting, indirect erythrocyte agglutination and Ouchterlony diffusion for IgG-binding activity. With all treatments IgG-binding peptides were extracted. However, no homogenous IgG-binding material was released by the enzymes tested. In each case a multiple peptide pattern with IgG-binding activity was found. The molecular weights of the active peptides released also differed between the extraction procedures. The isoelectric points between 4.0 and 4.3 of IgG-binding components were found to be similar for all three extracts." @default.
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- W1997161821 date "1987-07-01" @default.
- W1997161821 modified "2023-10-12" @default.
- W1997161821 title "Extraction of group C streptococcal IgG-binding receptor and characterization of the active peptides by Western blotting and isoelectric focusing" @default.
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- W1997161821 doi "https://doi.org/10.1016/s0176-6724(87)80262-6" @default.
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