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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1998-10-22
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pubmed:abstractText |
1. 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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0306-3623
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
277-82
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:9688472-Animals,
pubmed-meshheading:9688472-Annexins,
pubmed-meshheading:9688472-Anticoagulants,
pubmed-meshheading:9688472-Blood Coagulation,
pubmed-meshheading:9688472-Calcium,
pubmed-meshheading:9688472-Endopeptidases,
pubmed-meshheading:9688472-Factor X,
pubmed-meshheading:9688472-Humans,
pubmed-meshheading:9688472-Peptides,
pubmed-meshheading:9688472-Phosphatidylserines,
pubmed-meshheading:9688472-Protein Binding,
pubmed-meshheading:9688472-Prothrombin,
pubmed-meshheading:9688472-Starfish
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pubmed:year |
1998
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pubmed:articleTitle |
Analysis for sites of anticoagulant action of plancinin, a new anticoagulant peptide isolated from the starfish Acanthaster planci, in the blood coagulation cascade.
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pubmed:affiliation |
Department of Pharmacology, School of Medicine, Faculty of Medicine, University of the Ryukyus, Okinawa, Japan.
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pubmed:publicationType |
Journal Article
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