Production in vitro and properties of a modified form of bovine antithrombin, cleaved at the active site by thrombin.

This publication has 45 references indexed in Scilit:

• Immunological Evidence for a Proteolytic Cleavage at the Active Site of Antithrombin in the Mechanism of Inhibition of Coagulation Serine Proteases
  European Journal of Biochemistry, 1981
• The site in human antithrombin for functional proteolytic cleavage by human thrombin
  FEBS Letters, 1981
• Slow, spontaneous dissociation of the antithrombin—thrombin complex produces a proteolytically modified form of the inhibitor
  FEBS Letters, 1980
• Evidence by Chemical Modification for the Involvement of One or More Tryptophanyl Residues of Bovine Antithrombin in the Binding of High‐Affinity Heparin
  European Journal of Biochemistry, 1979
• The thrombin cleavage site in bovine antithrombin
  FEBS Letters, 1979
• The production of an inactive form of antithrombin through limited proteolysis by thrombin
  FEBS Letters, 1979
• Anticoagulant activity of heparin: Separation of high‐activity and low‐activity heparin species by affinity chromatography on immobilized antithrombin
  FEBS Letters, 1976
• The separation of active and inactive forms of heparin
  Biochemical and Biophysical Research Communications, 1976
• Protein inhibitors of proteolytic enzymes
  Accounts of Chemical Research, 1974
• Computed circular dichroism spectra for the evaluation of protein conformation
  Biochemistry, 1969