| Autor: |
Ohkuni H; Division of Immunology, Nippon Medical School, Kawasaki, Japan. h-okuni@nms.ac.jp, Todome Y, Okibayashi F, Watanabe Y, Ohtani N, Ishikawa T, Asano G, Kotani S |
| Jazyk: |
angličtina |
| Zdroj: |
FEMS immunology and medical microbiology [FEMS Immunol Med Microbiol] 1997 Feb; Vol. 17 (2), pp. 121-9. |
| DOI: |
10.1111/j.1574-695X.1997.tb01004.x |
| Abstrakt: |
A human blood platelet aggregation factor was purified from the extracellular products (ECP) of Streptococcus mitis, strain Nm-65 by sequential chromatography on DEAE-Sepharose CL-6B, hydroxyapatite and Superdex 75 columns. The purified factor (S. mitis-derived human platelet aggregation factor, Sm-hPAF) gave a single band with a molecular weight of 66 kDa on SDS-polyacrylamide gel electrophoresis (SDS-PAGE). Sm-hPAF showed a peak absorption at 278 nm and an isoelectric point of around 8.5. Chemical analyses revealed that Sm-hPAF contained no sugars and that its first 15 amino-terminal amino acid residues were H-DEQGNRPVETENIAR. Platelet aggregation activity of Sm-hPAF was abolished by heating at 45 degrees C for 10 min. Platelet aggregation by Sm-hPAF was accompanied by a release of prostaglandin E2 (PGE2) in a dose-dependent manner. The platelet aggregation was not inhibited by either prostaglandin E1 (PGE1) or Gly-Arg-Gly-Asp-Ser (GRGDS), that inhibit the platelet aggregation induced by collagen. Twenty (77%) platelet rich-plasma (PRP) specimens derived from 26 healthy volunteers were aggregated by Sm-hPAF, but the remaining 6 (23%) were not reactive. A preliminary study suggested the presence of an inhibitory factor against Sm-hPAF in the plasma from a non-reactive donor. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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