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- W1983758317 abstract "H UMAN ANTITHROMBIN III is a single chain plasma glycoprotein of molecular mass of approximately 60,000 daltons. I -3 It is the primary inhibitor of the activated clotting factors lIa/·4 IXa,5 Xa,5,6 XIa,7 Xlla,8 as well as kallikrein,9 plasmin,1O urokinase,l1 and trypsin. 12 The most important function of antithrombin ill is the inhibition of thrombin, which is relatively slow under physiologic conditions, but greatly accelerated in the presence of heparin. 13-16 Human plasma antithrombin III comprises 432 amino acid residues, 4 N-linked oligosaccharide side chains (for a total carbohydrate content of approximately 15%), and 3 disulphide bonds.3,l7,18 The tertiary structure, as determined by peptide modeling of the amino acid sequence and by analogy with the structure of human alpha-I-antitrypsin, consists of 31% alpha helix, 16% beta sheet, 9% beta turn, and 44% random coil. 19,20 Antithrombin III is synthesized in the liver and is a member of a family of serine protease inhibitors and related molecules that are referred to as the serpins. The history of the elucidation of antithrombin III as an inhibitor of coagulation has been extensively reviewed elsewhere2 and will be summarized only briefly in this article. The existence of a circulating anticoagulant was first postulated when it was noted that thrombin added to plasma lost its activity, progressively over time.2,24 This antithrombin activity was given the name progressive antithrombin activity. With the isolation, purification, and subsequent clinical use of heparin in the 1930s, it was found that heparin had the ability," @default.
- W1983758317 created "2016-06-24" @default.
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- W1983758317 date "1989-10-01" @default.
- W1983758317 modified "2023-09-25" @default.
- W1983758317 title "The Molecular Pathology of Inherited Human Antithrombin III Deficiency" @default.
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