Why the study?
Does protamine sulfate inhibit thrombin and its inactivation by ATIII in vitro?
Does protamine sulfate inhibit thrombin and its inactivation by ATIII in vitro?
Protamine sulfate demonstrates intrinsic anticoagulant activity by inhibiting thrombin's conversion of fibrinogen to fibrin and interfering with thrombin inactivation by ATIII.
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Protamine's in vitro thrombin effects warrant caution in heparin reversal; leaves open clinical relevance pending human data.
Protamine sulfate (salmine), a basic protein with a molecular weight of 4,626 +/- 109, is a known antiheparin agent which in the absence of heparin demonstrates an anticoagulant activity. To date, much work has been done to elucidate the interaction of heparin with thrombin and its physiologic inhibitor, Antithrombin III (ATIII). Little is known, however, about the mechanism of anticoagulant action of protamine sulfate and its mode of thrombin inactivation. We provide information about the interaction of protamine sulfate with purified, labeled thrombin and ATIII through binding experiments in which protamine is shown to inhibit the inactivation of thrombin by ATIII. Furthermore, we show in clotting assays that protamine sulfate has an inhibitory effect on thrombin in the conversion of fibrinogen to fibrin, and that this inhibition is concentration dependent, partial, and reversible.
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Cobel-Geard et al. (1983) studied this question.
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