Preparation and stability of a highly purified human thrombin standard.
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Biomedical subjects
Publications and source records attributed to M Miller-Andersson.
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The rapid loss in clotting activity of commercially available thrombins during storage is not reflected by their activity as measured by synthetic chromogenic substrates. It is suggested that conformational changes occurring during storage can affect the binding sites of thrombin for fibrinogen, whereas small synthetic substrates are incapable of monitoring these changes.
Potency estimations of thrombin have been performed using clotting and synthetic substrates in parallel assays. The International Standard and the Nordic Standard of thrombin have both been used as references. Divergencies in estimated unitage necessitated a study on possible heterogeneities in the standard preparations presented in this paper.
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Antithrombin III, purified to homogeneity according to polyacrylamide gel disc electrophoresis and immunoelectrophoresis, inhibited the activity of purified factor IXa and Xa, whereas factor VII was not inhibited either in the active or in the native form. Antithrombin III is the single most important inhibitor of factor Xa in plasma. Factor Xa does not, however, reduce the activity of antithrombin III against thrombin.
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