Feb 1, 1984

Evaluation of critical groups required for the binding of heparin to antithrombin

Proceedings of the National Academy of Sciences of the United States of America
D H AthaR D Rosenberg

Abstract

We have examined the quantitative importance of various monosaccharide residues of an octasaccharide domain of heparin that are responsible for the binding of this oligosaccharide to antithrombin. Different fragments of the octasaccharide were prepared by enzymatic digestion and the avidities of these oligosaccharides for antithrombin were determined by equilibrium dialysis. The data show that the non-reducing-end and the reducing-end tetrasaccharides contribute equally to the binding energy of the octasaccharide. The O6-sulfate group of the N-acetyl glucosamine moiety within the nonreducing-end tetrasaccharide is responsible for approximately equal to 45% of the binding energy of the octasaccharide. Neither the two non-sulfated uronic acid groups that flank this residue nor the N-sulfated glucosamine residue on the reducing end of this tetrasaccharide sequence that bears the unique O3-sulfate substituent contribute significantly to the binding energy of the octasaccharide. We suggest that the lack of sulfation of the two uronic acid moieties within the nonreducing-end tetrasaccharide may be required to permit the N-acetyl glucosamine O6-sulfate group to interact with a specific region on the antithrombin molecule. However, we ...Continue Reading

  • References18
  • Citations51

Mentioned in this Paper

N-Acetyl Glucosamide Measurement
Heparin
Structure-Activity Relationship
Liquaemin
Glucosamine
Uronic Acids
Digestion
Heparin, porcine
Fragments
Oligosaccharides

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