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Hideo Yoshizaki, Koichi Arai, Toshimi Mizoguchi, Masami Shiratsuchi, Yukio Hattori, Takao Nagoya, Yoshihiro Shidara, Masahiro Maki, Isolation and Characterization of an Anticoagulant Protein from Human Placenta, The Journal of Biochemistry, Volume 105, Issue 2, February 1989, Pages 178–183, https://doi.org/10.1093/oxfordjournals.jbchem.a122636
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Abstract
An anticoagulant protein was purified from the EDTA extract of human placental tissue. The purified protein had a molecular weight of 73, 000 on sodium dodecyl sulfate poly-acrylamide gel electrophoresis under both reducing and non-reducing conditions. Because this protein had the ability to bind phospholipids such as phosphatidylserine, phosphatidylinositol, and cardiolipin in the presence of Ca2+, this protein was designated as calphobindin II (CPB-II). CPB-II prolonged the clotting time of normal plasma when coagulation was induced by tissue factor, cephalin and ellagic acid or recalcification, but did not affect thrombin-initiated fibrin formation. CPB-II also inhibited the activation of prothrombin by the complete prothrombinase complex or factor Xa-phospholipid-Ca2+ but not that by phospholipid-free factor Xa. In addition, CPB-II had an inhibitory activity against phospholipase A2.