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Abstract

Antithrombin Rouen-II, a new inherited variant of antithrombin-III, was found in two members of a family with no definite history of thrombosis. The subjects had normal antigenic concentrations of antithrombin and normal progressive inhibitory activity. However, the variant had defective heparin and heparan sulfate cofactor activities, and was not activated by a synthetic pentasaccharide representing the minimum heparin sequence. The abnormal antithrombin was isolated using heparin-Sepharose chromatography, and on electrophoresis at pH 8.6 migrated more anodally than normal. Two-dimensional peptide mapping of tryptic and Staphylococcus aureus V8 protease digests was performed and the abnormal peptide was located by tryptophan staining. Amino acid sequence studies demonstrated a substitution of arginine at residue 47 by a serine. Evidence strongly suggests that arginine 47 is a prime heparin binding site in antithrombin and that it forms part of a proposed positively charged linear site (to which heparin binds) that stretches across the surface of the molecule from the A to the D helix.

Authors

J Y Borg, M C Owen, C Soria, J Soria, J Caen, R W Carrell

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Citations to this article in year 1997 (3)

Title and authors Publication Year
The anticoagulant activation of antithrombin by heparin
L Jin, JP Abrahams, R Skinner, M Petitou, RN Pike, RW Carrell
Proceedings of the National Academy of Sciences of the United States of America 1997
BIOCHEMICAL AND PHARMACOLOGIC RATIONALE FOR THE DEVELOPMENT OF A SYNTHETIC HEPARIN PENTASACCHARIDE
JM Walenga, WP Jeske, L Bara, MM Samama, J Fareed
Thrombosis Research 1997
The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site
R Skinner, JP Abrahams, JC Whisstock, AM Lesk, RW Carrell, MR Wardell
Journal of Molecular Biology 1997

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