Isolation and characterization of an anticoagulant protein from human placenta.
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 polyacrylamide 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.
Yoshizaki
H
H
Tokyo Research Laboratories, Kowa Co., Ltd.
Arai
K
K
Mizoguchi
T
T
Shiratsuchi
M
M
Hattori
Y
Y
Nagoya
T
T
Shidara
Y
Y
Maki
M
M
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D017302:Annexins; D000911:Antibodies, Monoclonal; D001777:Blood Coagulation; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D066298:In Vitro Techniques; D007457:Iodine Radioisotopes; D051379:Mice; D008807:Mice, Inbred BALB C; D010741:Phospholipases A / Q000032:analysis / Q000378:metabolism; D054467:Phospholipases A2; D010743:Phospholipids / Q000032:analysis; D010920:Placenta / Q000032:analysis*; D011247:Pregnancy; D011257:Pregnancy Proteins / Q000302:isolation & purification*
D000596:Amino Acids; D017302:Annexins; D000911:Antibodies, Monoclonal; D007457:Iodine Radioisotopes; D010743:Phospholipids; D011257:Pregnancy Proteins; D010741:Phospholipases A; D054467:Phospholipases A2