Open AccessThe Characteristics of M Proteins Purified by Column Chromatography With Hydroxyapatite from Acid Extracts of Streptococcus Pyogenes of Types 1, 3, 6, 12 and 17
Author(s) -
Kenneth L. Vosti
Publication year - 1978
Publication title -
journal of medical microbiology/journal of medical microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.91
H-Index - 117
eISSN - 1473-5644
pISSN - 0022-2615
DOI - 10.1099/00222615-11-4-453
Subject(s) - streptococcus pyogenes , antigen , elution , chromatography , molecular mass , amino acid , ammonium , chemistry , biochemistry , column chromatography , biology , microbiology and biotechnology , bacteria , staphylococcus aureus , immunology , organic chemistry , genetics , enzyme
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.