Abstract
M protein of group A streptococci was extracted by mild peptic digestion. Optimal amounts of type specific M protein were released after 20 min of digestion with 0.02 mg of pepsin per ml at pH 5.8. Immunological analysis revealed that, unlike conventional HCl extracts, pepsin extracts lacked the surface C carbohydrate antigen and contained less non type specific, heat stable cellular antigens; they also lacked detectable heat labile T protein. Similar to HCl extracts, however, the pepsin extracted M protein precipitated homologous type M antisera and inhibited type specific opsonization of homologous group A streptococci. Furthermore, the pepsin extract was capable of inducing type specific opsonic M antibody in rabbits. This method may provide a useful initial step in the purification of M protein by reducing contaminating antigens.
Original language | English |
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Pages (from-to) | 891-896 |
Number of pages | 6 |
Journal | Infection and Immunity |
Volume | 9 |
Issue number | 5 |
State | Published - 1974 |
Externally published | Yes |