The Journal of Medical Microbiology, Vol 11, Issue 4 453-462, Copyright © 1978 by Society for General Microbiology
The characteristics of M proteins purified by column chromatography with hydroxyapatite from acid extracts of Streptococcus pyogenes of types 1, 3, 6, 12 and 17
K. L. Vosti
Purified M proteins were recovered from acid extracts of Streptococcus
pyogenes, M-types 1, 3, 6, 12 and 17, by elution from columns of
hydroxyapatite of the proteins precipitated with ammonium sulphate. M
protein free from non-type-specific antigens was recovered only from M-type
12. Although similar fractions were not recovered from M-types 1, 3, 6 and
17, purified preparations containing a single cross-reactive antigen were
obtained. In addition to the M proteins associated with cross-reactive
antigens, type-specific antigens that did not stimulate opsonic antibodies
were isolated from revealed molecular weights that ranged from 32,000 to
63,000 daltons, total amino acid compositions that were similar, and
N-terminal amino acids that were variable.
