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Nature of the Inhibition of Prothrombin Consumption by Lysed Fibrinogen
Author(s) -
Triantaphyllopoulos D. C.,
Chen C.,
Triantaphyllopoulos E.
Publication year - 1969
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1969.tb00439.x
Subject(s) - fibrinogen , thrombin , chemistry , platelet , coagulation , biochemistry , fibrin , lysis , ammonium , factor x , medicine , chromatography , endocrinology , immunology , organic chemistry
Summary: The derivatives of the fibrinolytic digestion of fibrinogen which precipitate between 25 and 50 per cent ammonium sulphate saturation inhibit the prothrombin consumption of blood. Disintegration of the platelets by freeze‐thawing or sonication or addition of purified platelet factor 3 did not normalize prothrombin consumption. Normalization occurred after addition of an excess of platelet factor 3 or brain phospholipid. These findings suggest that lysed fibrinogen inhibits the action rather than the release of platelet factor 3. The anticoagulant activity varied neither with the degree of digestion of the parent fibrinogen solution nor with the electrophoretic fraction of the fibrinogen derivatives in contradistinction to the antithrombic effect, which has been shown to depend on these parameters. In purified systems the 25–50 per cent ammonium sulphate fraction of the fibrinogen derivatives retarded the degradation of prothrombin by thrombin and more thrombin activity was found in the two‐stage assay.