[HTML][HTML] On the mechanism of the antifibrinolytic activity of plasma carboxypeptidase B
DV Sakharov, EF Plow, DC Rijken - Journal of Biological Chemistry, 1997 - ASBMB
The precursor of plasma carboxypeptidase B (pCPB) also known as thrombin-activable
fibrinolysis inhibitor can be converted by thrombin to an active enzyme capable of
eliminating C-terminal Lys-and Arg-residues from proteins. The activation is about 1000-fold
more efficient in the presence of thrombomodulin (TM). We investigated the antifibrinolytic
potency of maximally activated pCPB in plasma and explored the antifibrinolytic mechanism
of pCPB. During clotting of plasma in the presence of 3.3 NIH units/ml thrombin and 1 μg/ml …
fibrinolysis inhibitor can be converted by thrombin to an active enzyme capable of
eliminating C-terminal Lys-and Arg-residues from proteins. The activation is about 1000-fold
more efficient in the presence of thrombomodulin (TM). We investigated the antifibrinolytic
potency of maximally activated pCPB in plasma and explored the antifibrinolytic mechanism
of pCPB. During clotting of plasma in the presence of 3.3 NIH units/ml thrombin and 1 μg/ml …