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Armstrong, S.A., Husten, E.J., Esmon, C.T. and Johnson, A.E. (1990) The Active Site of Membrane-Bound Meizothrombin. A Fluorescence Determination of Its Distance from Phospholipids Surface and Its Conformational Sensitivity to Calcium and Factor Va. The Journal of Biological Chemistry, 265, 6210-6218.

has been cited by the following article:

• TITLE: Meizothrombin Preparation and Its Role in Fibrin Formation and Platelet Aggregation

  AUTHORS: Dar’ya S. Korolova, Tamara M. Chernyshenko, Olga V. Gornytska, Volodymyr O. Chernyshenko, Tatiana N. Platonova

  KEYWORDS: Prothrombin, Meizothrombin, Platelets, Fibrin Polymerization

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.5 No.7, June 5, 2014

  ABSTRACT: Meizothrombin (MT) is one of prothrombin derivatives which appears in haemostasis activation area. However, its role in haemostasis regulation isn’t clear. We studied the role of MT in fibrin formation, platelet activation and aggregation. A new effective method of obtaining MT from native human prothrombin was developed using immobilised prothrombin activator from Echis multisquamatis venom. The protein was stable and electrophoretically pure. Platelet-rich plasma for aggregation study and gel-sieved platelets for flow-cytometry were separated from blood of healthy donors. It was shown that MT transformed fibrinogen to fibrin and activated clotting factor XIII. MT didn’t activate gel-sieved intact platelets, but in platelet-rich plasma, increased platelet aggregation induced by ADP, collagen and adrenalin.