Isolation and partial purification of a novel anticoagulant from arteries of human umbilical cord
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32
摘要：
An anticoagulant fraction was isolated from the homogenate of human umbilical cord arteries, using Sephadex gel filtration and DEAE-Sephacel chromatography. Analysis with dodecyl sulfate/polyacrylamide gel electrophoresis and inactivation studies using proteolytic enzymes indicate that the anticoagulant activity is associated with a polypeptide with an apparent M r of 32000. The anticoagulant inhibits thromboplastin as well as factor X a induced clotting but does not affect thrombin initiated fibrin formation. The anticoagulant inhibits the activation of prothrombin by the complete prothrombinase complex, by phospholipid bound factor X a but not by free factor X a . The inhibition is instantaneous and independent of the incubation time over the whole range of concentrations tested. Therefore, the anticoagulant is unlikely to be a phospholipase or a protease. Its action does not resemble that of the plasma protease inhibitors, but it probably interferes with the phospholipidclotting factor interactions.
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DOI：
10.1111/j.1432-1033.1985.tb09150.x
被引量：
年份：
2010
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