A disulfide bond in antithrombin is required for heparin-accelerated thrombin inactivation.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference28 articles.
1. Highly Purified Antithrombin III with Heparin Cofactor Activity Prepared by Disc Electrophoresis
2. Identity of Plasma-activated Factor X Inhibitor with Antithrombin III and Heparin Cofactor
3. The Inhibition of Human Plasmin by Human Antithrombin-Heparin Cofactor
4. Inhibition of human factor IXa by human antithrombin
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1. Insight into Residues Critical for Antithrombin Function from Analysis of an Expanded Database of Sequences That Includes Frog, Turtle, and Ostrich Antithrombins;Journal of Proteome Research;2002-06-14
2. The native metastable fold of C1-inhibitor is stabilized by disulfide bonds;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;2000-08
3. Effect of aPMR1 disruption on the processing of heterologous glycoproteins secreted in the yeastSaccharomyces cerevisiae;Biotechnology and Bioprocess Engineering;2000-08
4. Heparin Binding Domain of Human Antithrombin III Inferred from the Sequential Reduction of Its Three Disulfide Linkages;Journal of Biological Chemistry;1989-07
5. Physicochemical Aspects of Heparin Cofactor II;Annals of the New York Academy of Sciences;1989-06
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