1979
DOI: 10.1128/iai.24.3.637-641.1979
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Surface protein of a Streptococcus agalactiae isolate

Abstract: A Streptococcus agalactiae isolate of bovine origin was cultured in broth; log-phase cells were washed and radioiodinated and subsequently extracted at low pH in the presence of a nonionic detergent. A protein antigen was purified from concentrated extract by ultracentrifugation, gel filtration, and ion-exchange chromatography. The molecular weight of the protein was estimated at 31,800. The agglutinogenic character of the protein indicated its localization at the cell surface.

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Cited by 5 publications
(2 citation statements)
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“…Binding studies. Binding of radiolabeled fibrinogen to 60 beta-hemolytic group B and 40 group D streptococcal strains was measured in a standardized assay by using 0.4 jig of labeled protein added to 4 x 105 bacterial cells. In this assay fibrinogen was found to bind to 6 of 60 group B strains studied (strains SB1, SB2, SB3, SB35, SB55, and SB60; Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Binding studies. Binding of radiolabeled fibrinogen to 60 beta-hemolytic group B and 40 group D streptococcal strains was measured in a standardized assay by using 0.4 jig of labeled protein added to 4 x 105 bacterial cells. In this assay fibrinogen was found to bind to 6 of 60 group B strains studied (strains SB1, SB2, SB3, SB35, SB55, and SB60; Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Although useful taxonomically, the function of these proteins has not been described. A 31-kd surface protein has also been reported in group B streptococci (13), and three proteins, of unknown function, have been found in S. mutans (32).…”
Section: Discussionmentioning
confidence: 99%