Fig. 3.
Fig. 3. Comparison of a prethrombin 2, thrombin B chain, TAT complex formation, and the quantitation of covalently bound thrombin. / (A) Data were collected from 8 experiments for the prothrombin fragments and 35 experiments for TAT formation. The prethrombin 2 (●) has an initiation phase duration of 2.8 minutes and increases at a rate of propagation of 52.1 ± 2.0 nM/min. Maximum levels attained are 549 ± 86 nM. α-thrombin B chain (□) formation has a slightly longer initiation phase duration of 3.6 ± 0.2 minutes and increases at a comparable rate of 56.9 ± 2.1 nM/min, reaching maximum levels of 494 ± 66 nM by 20 minutes. The TAT (⧫) composite has an initiation phase duration up to 4.6 ± 0.6 minutes with an increasing rate of propagation of 83.9 ± 3.8 nM/min. The detected maximum level reached was 851 ± 53 nM TAT. (B) TAT complex formation (ELISA)–thrombin B chain (immunoblot) is shown (⧫, nM) versus time over the course of 20 minutes.

Comparison of a prethrombin 2, thrombin B chain, TAT complex formation, and the quantitation of covalently bound thrombin.

(A) Data were collected from 8 experiments for the prothrombin fragments and 35 experiments for TAT formation. The prethrombin 2 (●) has an initiation phase duration of 2.8 minutes and increases at a rate of propagation of 52.1 ± 2.0 nM/min. Maximum levels attained are 549 ± 86 nM. α-thrombin B chain (□) formation has a slightly longer initiation phase duration of 3.6 ± 0.2 minutes and increases at a comparable rate of 56.9 ± 2.1 nM/min, reaching maximum levels of 494 ± 66 nM by 20 minutes. The TAT (⧫) composite has an initiation phase duration up to 4.6 ± 0.6 minutes with an increasing rate of propagation of 83.9 ± 3.8 nM/min. The detected maximum level reached was 851 ± 53 nM TAT. (B) TAT complex formation (ELISA)–thrombin B chain (immunoblot) is shown (⧫, nM) versus time over the course of 20 minutes.

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