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pubmed-article:9688472pubmed:abstractText1. Effects of plancinin, a new anticoagulant peptide, on the human blood coagulation cascade were investigated. 2. Plancinin prolonged both activated partial thromboplastin time and prothrombin time, and it significantly inhibited factor X activation by both intrinsic (factor IXa-factor VIIIa-phospholipids-Ca2+) and extrinsic (factor VIIa-tissue factor-phospholipids-Ca2+) tenase complexes and prothrombin activation by prothrombinase complex (factor Xa-factor Va-phospholipids-Ca2+) to 13.8%, 4.8% and 10.5% of control value, respectively. 3. Results indicate that sites of anticoagulant action of plancinin may be located in activation steps of prothrombin and factor X.lld:pubmed
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pubmed-article:9688472pubmed:dateRevised2004-11-17lld:pubmed
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pubmed-article:9688472pubmed:articleTitleAnalysis for sites of anticoagulant action of plancinin, a new anticoagulant peptide isolated from the starfish Acanthaster planci, in the blood coagulation cascade.lld:pubmed
pubmed-article:9688472pubmed:affiliationDepartment of Pharmacology, School of Medicine, Faculty of Medicine, University of the Ryukyus, Okinawa, Japan.lld:pubmed
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