PubMed · 7078951
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G Sas. 1982-04-18. [Antithrombin III. Antithrombin].. https://pubmed.ncbi.nlm.nih.gov/7078951/
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Autoproteolysis of blood coagulation factor Xa (FXa) results in the excision of a 4-kDa fragment (beta-peptide) from the intact subform, factor Xaalpha (FXaalpha), to yield factor Xabeta (FXabeta). In the preceding paper, we showed that generation of FXabeta leads to expression of a plasminogen binding site. FXabeta may consequently participate in fibrinolysis; therefore, the timing of subform conversion compared with thrombin production is important. In the current study we evaluated the kinetics of FXabeta generation, which showed that autoproteolysis of FXaalpha followed a second order mechanism where FXaalpha and FXabeta behaved as identical enzymes. Rate constants of 9 and 172 M-1 s-1 were derived, respectively, in the absence and presence of FXaalpha binding to procoagulant phospholipid. Under identical conditions the latter is estimated to be 6 orders of magnitude slower than thrombin generation by prothrombinase. Since heparin binding and prothrombin recognition have been previously attributed to a region of FXaalpha proximal to the beta-peptide, functional comparisons were conducted using homogeneous and stabilized preparations of FXaalpha and FXabeta. Comparisons included 1) the recognition of small substrates; 2) the rate of interaction with antithrombin/heparin; 3) the assembly of prothrombinase; and 4) the activation of prothrombin by prothrombinase. Although the beta-peptide neighbors a probable functional region in FXaalpha, conversion to FXabeta was not observed to influence these functions. The data support a model where FXaalpha is predominantly responsible for thrombin generation and where slow conversion to FXabeta coordinates coagulation and the initiation of fibrinolysis at sites of prothrombinase assembly.
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