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October 1, 1996Journal of Biological ChemistryOpen Access

Binding of Fibrin Monomer and Heparin to Thrombin in a Ternary Complex Alters the Environment of the Thrombin Catalytic Site, Reduces Affinity for Hirudin, and Inhibits Cleavage of Fibrinogen

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Authors

PHPhilip J. HoggUniversity of Technology SydneyCJCraig M. JacksonUniversity of San DiegoJLJan K. LabanowskiUniversity of Notre Dame

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Cite This Study

Hogg et al. (1996) studied this question.

synapsesocial.com/papers/6a771d477ecc675f86ae3c5chttps://doi.org/10.1074/jbc.271.42.26088
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Formation of a ternary complex between thrombin, fibrin monomer, and heparin influences the action of thrombin on its substrates.1990 · 50 citations
  2. 2Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects.1991 · 221 citations
  3. 3Clotting of bovine fibrinogen. Kinetic analysis of the release of fibrinopeptides by thrombin and of the calcium uptake upon clotting at high fibrinogen concentrations1988 · 40 citations
  4. 4The Structure of a Complex of Recombinant Hirudin and Human α-Thrombin1990 · 715 citations
  5. 5Steady state kinetic parameters for the thrombin-catalyzed conversion of human fibrinogen to fibrin.1983 · 154 citations