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. 1980 Sep;29(3):999–1006. doi: 10.1128/iai.29.3.999-1006.1980

Affinity purification and characterization of protease-susceptible antigen I of Streptococcus mutans.

M W Russell, E D Zanders, L A Bergmeier, T Lehner
PMCID: PMC551230  PMID: 7000709

Abstract

An antigenic component (antigen I) of the cell surface of Streptococcus mutans has been purified from culture supernatants and shown to be immunologically identical to the protease-susceptible moiety of antigen I/II. Ion-exchange and gel filtration chromatography failed to yield a physicochemically homogeneous product. Immunoasbsorbent chromatography on single and tandem columns containing immobilized antibodies to antigens I/II and II yielded identical products which were homogeneous in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and which when injected into rabbits induced monospecific antisera to antigen I. This antigen consisted of approximately 70% protein. Its molecular weight was estimated as 150,000, and the isoelectric point was estimated to be 5.1. Immunofluorescence microscopy using monospecific antiserum to antigen I showed that a similar antigen was present on cells of S. mutans serotypes a, c, d, e, f, and g, but not b.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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