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Site‐directed mutagenesis of alanine‐382 of human...
Journal article

Site‐directed mutagenesis of alanine‐382 of human antithrombin III

Abstract

Antithrombin III Hamilton is a structural variant of antithrombin III (AT-III) with normal heparin affinity but impaired serine protease inhibitory activity. The molecular defect of AT-III-Hamilton is a substitution of threonine for alanine at amino acid residue 382. Recently it has been shown that both plasma-derived and cell-free-derived AT-III-Hamilton polypeptides act as substrates rather than inhibitors of thrombin and factor Xa. In the …

Authors

Austin RC; Rachubinski RA; Blajchman MA

Journal

FEBS Letters, Vol. 280, No. 2, pp. 254–258

Publisher

Wiley

Publication Date

March 25, 1991

DOI

10.1016/0014-5793(91)80305-m

ISSN

0014-5793