The multiple molecular structure of the M proteins of group A streptococci.

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Abstract
Highly purified M proteins of 3 serotypes of group A streptococci have been analyzed by physical, chemical, and serological techniques. These antigens appearing homogeneous in ultracentrifugation and immunodiffusion analyses exhibit a unique multiple molecular structure when observed by gel electrophoresis. The multiple structures within each serotype of M protein are antigenically identical and exhibit similar electrophoretic patterns from strains of streptococci of homologous serotypes. No displacement of electro-phoresed bands has been observed in 8 [image]urea, and amino acid analyses of isolated fractions have not revealed the structural relationship of the units within the antigenic complex.