Characteristics of a high molecular weight extracellular protein of Streptococcus mutans
| Autor: | Neil Hunter, Kenneth W. Knox, Henry Forester |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Antiserum
Antigenicity Antigens Bacterial Immunodiffusion Strain (chemistry) Immune Sera Myocardium Biology Cross Reactions biology.organism_classification Microbiology Streptococcus mutans Serology Molecular Weight Antigen biology.protein Extracellular Animals Glucosyltransferase Electrophoresis Polyacrylamide Gel Rabbits Amino Acids |
| Zdroj: | Journal of general microbiology. 129(9) |
| ISSN: | 0022-1287 |
| Popis: | Summary: A high molecular weight protein antigen, designated P1, has been isolated from the culture fluid of chemostat-grown Streptococcus mutans strain Ingbritt and shown to be free of other antigens including glucosyltransferase. Antiserum against the protein was used in rocket immunoelectro-phoresis to confirm and extend the previous observation that there were major differences in the amount of the protein produced under different growth conditions. Physico-chemical and serological studies indicated that protein P1 was indistinguishable from antigens B, I II and IF isolated in other laboratories. Mammalian tissue cross-reactivity of protein P1 was demonstrated by binding of antiserum to P1 to sections of normal rabbit tissues, particularly heart. There was also a statistically significant increase in the number of mononuclear leucocytes in heart tissue of rabbits which had been injected with protein P1, when compared with the levels in control uninjected rabbits; injection with whole cells of S. mutans Ingbritt did not produce this effect. |
| Databáze: | OpenAIRE |
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