Heparin-dependent Modification of the Reactive Center Arginine of Antithrombin and Consequent Increase in Heparin Binding Affinity

This publication has 25 references indexed in Scilit:

• Biological implications of a 3 å structure of dimeric antithrombin
  Structure, 1994
• [30] Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin
  Published by Elsevier ,1993
• P1 variant antithrombins Glasgow (393 Arg to His) and Pescara (393 Arg to Pro) have increased heparin affinity and are resistant to catalytic cleavage by elastase Implications for the heparin activation mechanism
  FEBS Letters, 1991
• Implications of the three-dimensional structure of .alpha.1-antitrypsin for structure and function of serpins
  Biochemistry, 1989
• Antithrombin Glasgow, 393 arg to his: A P₁ reactive site variant with increased heparin affinity but no thrombin inhibitory activity
  FEBS Letters, 1988
• Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
  Analytical Biochemistry, 1987
• Heparin Promotes the Inactivation of Antithrombin by Neutrophil Elastase
  Science, 1987
• A simple two-step procedure for the isolation of antithrombin III from biological fluids
  Thrombosis Research, 1981
• Human leukocyte granule elastase: rapid isolation and characterization
  Biochemistry, 1976
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970