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- W2889300185 abstract "A fragment of human fibrinogen was obtained by a 30-min digest of fibrinogen with plasmin. The reaction was terminated by 10 mM diisopropyl fluorophosphate and the fragment obtained by sequential gel filtrations on Sephacryl S-200 and Bio Gel P-30. This fragment displayed a single band on both reduced and nonreduced SDS polyacrylamide electrophoreses with a relative Mr of ∼25,000. It did not crossreact with antisera against fibrinogen, fragment D or fragment E and suggested its sequestered location in native fibrinogen. An antiserum raised against this fragment reacted with the fragment itself as well as fibrinogen. Its amino acid composition and other properties suggested that it was derived from the Aa -chains of fibrinogen. The fragment had anticoagulant activity as it was able to inhibit thrombin time in a dose-dependent fashion and it could also inhibit the polymerization of fibrin monomers. However, radioactively labelled fragment was not able to bind calcium ions in equilibrium dialysis experiments, nor was it able to bind plasma fibrin clot, fibrinogen- or fibrin-bound Sepharose columns. The activation of plasminogen by streptokinase was inhibited by the fragment. On the other hand plasminogen activation by melanoma tissue plasminogen activator and urokinase were both enhanced in the presence of the fragment." @default.
- W2889300185 created "2018-09-07" @default.
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- W2889300185 date "1987-01-01" @default.
- W2889300185 modified "2023-10-01" @default.
- W2889300185 title "PROPERTIES OF A HUMAN FIBRINOGEN A α-CHAIN DEGRADATION FRAGMENT" @default.
- W2889300185 doi "https://doi.org/10.1055/s-0038-1643333" @default.
- W2889300185 hasPublicationYear "1987" @default.
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