Studies on the procoagulant activity of human amniotic fluid II. The role of factor VII

Partially purified Amniotic Fluid Factor (AFF) is found to directly activate human factor X, with a Km for factor X of 0.37 ± 0.06 M. Added phospholipid has only a slight effect on the activation at low concentrations, and inhibits the reaction at higher concentrations. Both DIPF and PMSF inhibit AF...

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Veröffentlicht in:Thrombosis research 1985-09, Vol.39 (5), p.571-585
Hauptverfasser: Pusey, Marc L., Mende, Thomas J.
Format: Artikel
Sprache:eng
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Zusammenfassung:Partially purified Amniotic Fluid Factor (AFF) is found to directly activate human factor X, with a Km for factor X of 0.37 ± 0.06 M. Added phospholipid has only a slight effect on the activation at low concentrations, and inhibits the reaction at higher concentrations. Both DIPF and PMSF inhibit AFF factor X activation. Although added phospholipid is not required for AFF-activity, phospholipase C rapidly destroys it, indicating the presence of intrinsic phospholipid. Phospholipase C treated AFF releases factor VII activity, which leads to the conclusion that AFF is in fact a thromboplastin: factor VII complex. Both AFF and a human brain thromoplastin factor VII complex prepared in vitro were inhibited by Zn ++ ion, while human brain thromboplastin alone is not. AFF is markedly larger than the human brain thromboplastin-factor VII complex as judged by gel filtration.
ISSN:0049-3848
1879-2472
DOI:10.1016/0049-3848(85)90237-3