Abstract
α 2-Plasmin inhibitor (α 2PI), also called α 2-antiplasmin, is a plasma glycoprotein which rapidly inactivates plasmin proteolytic activity (1). Its molecular weight, deduced from the cDNA sequence and the carbohydrate content (14%), is ≅ 58 KD (2) whereas the molecular weight estimated by SDS-gel electrophoresis was 67 KD (1). The cause of the discrepancy is not known. Its concentration in human plasma was estimated to be 6.9 ± 0.6 mg/100 ml (3), which is estimated to be ≅ 1.2 μM on the assumption of MW 58KD. α 2PI is a serine proteinase inhibitor (serpin) which is able to inhibit several different “serine” proteinases, but is mainly playing a role as a primary inhibitor of plasmin-mediated fibrinolysis (4). Its congenital deficiency results in a lifelong severe hemorrhagic tendency due to premature degradation of hemostatic plugs by physiologically occurring fibrinolytic process (4–7).
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Aoki, N. (1990). Molecular Genetics of Alpha 2 Plasmin Inhibitor. In: Liu, C.Y., Chien, S. (eds) Fibrinogen, Thrombosis, Coagulation, and Fibrinolysis. Advances in Experimental Medicine and Biology, vol 281. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3806-6_19
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DOI: https://doi.org/10.1007/978-1-4615-3806-6_19
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