title: [Isolation of calphobindin-II and its mechanism of anticoagulant activity].
abstract: In addition to calphobindin-I (a placental coagulation inhibitor), another anticoagulant protein (calphobindin-II) was isolated from the EDTA extract of human placenta. The purified protein had a molecular weight of 68,000 daltons according to sodium dodecyl sulfate polyacrylamide gel electrophoresis under both reduced and non-reduced conditions. This protein prolonged prothrombin time, activated partial thromboplastin time and recalcification time, but did not affect thrombin time. This substance also inhibited both factor X activation by a complex of [factor VII-tissue factor-Ca2+] and factor II activation by a complex of [factor Xa-phospholipid-Ca2+]. This protein was a stronger anticoagulant than calphobindin-I.
authors.affiliation: Department of Obstetrics and Gynecology, Akita University School of Medicine.
authors.forename: K
authors.initials: K
authors.lastname: Kume
mesh_terms: D017302:Annexins; D001777:Blood Coagulation / Q000187:drug effects*; D002118:Calcium / Q000097:blood; D004789:Enzyme Activation / Q000187:drug effects; D005170:Factor X / Q000378:metabolism; D005260:Female; D006801:Humans; D008970:Molecular Weight; D010314:Partial Thromboplastin Time; D010920:Placenta / Q000032:analysis; D011247:Pregnancy; D011257:Pregnancy Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D011516:Prothrombin / Q000378:metabolism; D011517:Prothrombin Time
chemical_list: D017302:Annexins; D011257:Pregnancy Proteins; D011516:Prothrombin; D005170:Factor X; D002118:Calcium