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Molecular Genetics of Alpha 2 Plasmin Inhibitor

  • Nobuo Aoki
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 281)

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).

Keywords

Crosslinking Site Congenital Deficiency Carbohydrate Side Chain Lysine Binding Site Coagulation Factor Xiii 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Nobuo Aoki
    • 1
  1. 1.The First Department of MedicineTokyo Medical and Dental UniversityTokyoJapan

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