Tick Anticoagulant Peptide (TAP) Is a Novel Inhibitor of Blood Coagulation Factor Xa

DOI Web Site 被引用文献15件
  • Lloyd Waxman
    Biological Chemistry Department, Merck Sharp & Dohme Research Laboratories, West Point, PA 19486.
  • Donna E. Smith
    Biological Chemistry Department, Merck Sharp & Dohme Research Laboratories, West Point, PA 19486.
  • Karen E. Arcuri
    Biological Chemistry Department, Merck Sharp & Dohme Research Laboratories, West Point, PA 19486.
  • Geroeg P. Vlasuk
    Biological Chemistry Department, Merck Sharp & Dohme Research Laboratories, West Point, PA 19486.

抄録

<jats:p> A low molecular weight serine protease inhibitor (TAP) was purified from extracts of the soft tick, <jats:italic>Ornithodoros moubata</jats:italic> . The peptide is a slow, tight-binding inhibitor, specific for factor Xa ( <jats:italic>K</jats:italic> <jats:sub>i</jats:sub> = 0.588 ± 0.054 n <jats:italic>M</jats:italic> ). The inhibitor also acts as an anticoagulant in several human plasma clotting assays in vitro. Its amino acid sequence (60 residues) has limited homology to the Kunitz-type inhibitors. However, unlike other inhibitors of this class, TAP inhibits only factor Xa. It had no effect at a 300-fold molar excess on factor VIIa, kallikrein, trypsin, chymotrypsin, thrombin, urokinase, plasmin, tissue plasminogen activator, elastase, or <jats:italic>Staphylococcus aureus</jats:italic> V8 protease. TAP's specificity and size suggest that it may have therapeutic value as an anticoagulant. </jats:p>

収録刊行物

  • Science

    Science 248 (4955), 593-596, 1990-05-04

    American Association for the Advancement of Science (AAAS)

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