Molecular Genetics of Alpha 2 Plasmin Inhibitor

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


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).


Crosslinking Site Congenital Deficiency Carbohydrate Side Chain Lysine Binding Site Coagulation Factor Xiii 
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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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