Abstract
A surface protein antigen of Streptococcus mutans having two sets of antigenic determinants (antigens I and II) was purified by column chromatography from culture supernatants of S. mutans serotype c. The protease-resistant component, antigen II, was purified from pronase-digested antigen I/II. The antigens were analyzed chemically and immunologically, and their physicochemical properties were investigated. Antigen I/II consisted of more than 80% protein, and its peptide chain molecular weight was estimated to be 185,000. Antigen II consisted of approximately 60% protein, with a peptide chain molecular weight of 48,000. Antisera to antigens I/II and II were raised in rabbits and used to investigate the presence of the antigens in cells of other streptococci. This indicated that not only serotype c but also serotypes e and f possessed antigen I and II determinants, whereas serotypes a, d, and g possessed a determinant related to antigen I but not one related to antigen II.
MeSH Terms
Amino Acids/analysis
Animals
Antigens, Bacterial/analysis,isolation & purification
Electrophoresis, Polyacrylamide Gel
Fluorescent Antibody Technique
Immune Sera
Molecular Weight
Peptide Hydrolases/analysis
Rabbits
Serotyping
Streptococcus mutans/immunology
Chemicals
Amino Acids
Antigens, Bacterial
Immune Sera
Peptide Hydrolases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Russell M W
Bergmeier L A
Zanders E D
Lehner T
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