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. 2008 Jul 1;47(30):7963–7974. doi: 10.1021/bi800593k

Figure 4.

Figure 4

Analysis of the activation of plasma-derived prothrombin by prothrombinase. Plasma-derived prothrombin (1.4 μM) was incubated in different mixtures with PCPS vesicles (20 μM), and prothrombinase assembled with either wild-type factor Va [(A) 10 nM] or factor VaΔ680−709 [(B) 10 nM] as described in , and the reaction was started by the addition of factor Xa. (C) Prothrombinase assembled with factor VaΔ680−709 in the presence of 20 μM DYDYQ (same conditions as in panel B). (D) Prothrombinase assembled with plasma-derived factor Va (10 nM). (E) Prothrombinase assembled with factor Va4A (10 nM). At selected time intervals, aliquots of the reaction mixtures were withdrawn and treated as described in . Lane M contained the molecular weight markers (from top to bottom): 98000, 64000, 50000, 36000, and 22000. Lanes 1−19 represent samples from the reaction mixture before (0 min) the addition of factor Xa and 20 s, 40 s, 60 s, 80 s, 100 s, 120 s, 140 s, 160 s, 180 s, 200 s, 220 s, 240 s, 5 min, 6 min, 10 min, 20 min, 30 min, and 60 min, respectively, following the addition of factor Xa. The prothrombin-derived fragments are shown as follows: II, prothrombin (amino acid residues 1−579); prethrombin-1 (amino acid residues 156−579); F1·2-A, fragment 1·2-A chain (amino acid residues 1−320); F1·2, fragment 1·2 (amino acid residues 1−271); P2, prethrombin-2 (amino acid residues 272−579); P2′, prethrombin-2 cleaved at Arg284; B, B chain of α-thrombin (amino acid residues 321−579).