Evidence by Chemical Modification for the Involvement of One or More Tryptophanyl Residues of Bovine Antithrombin in the Binding of High-Affinity Heparin-Reference-Cited by-同舟云学术

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Evidence by Chemical Modification for the Involvement of One or More Tryptophanyl Residues of Bovine Antithrombin in the Binding of High-Affinity Heparin

Published:1979-12 Issue:2 Volume:102 Page:497-502
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

BJORK Ingemar,NORDLING Kerstin

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1979.tb04265.x/fullpdf

Reference29 articles.

1. The separation of active and inactive forms of heparin

2. Anticoagulant activity of heparin: Separation of high-activity and low-activity heparin species by affinity chromatography on immobilized antithrombin

Cited by 42 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Importance of Tryptophan 49 of Antithrombin in Heparin Binding and Conformational Activation;Biochemistry;2005-08-09

2. Heparin-Binding Domains in Vascular Biology;Arteriosclerosis, Thrombosis, and Vascular Biology;2004-09

3. Thermodynamics of Charged Oligopeptide-Heparin Interactions;Biochemistry;1995-03-07

4. Defining the heparin-binding domain of antithrombin;Blood Coagulation & Fibrinolysis;1994-02

5. Non-specific influence of chemical modification upon the properties of antithrombin III:Modification of carboxyl groups;Thrombosis Research;1992-08

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