Hydrophobic residues 382-386 of antithrombin III, Ala-Ala-Ala-Ser-Thr, serve as the epitope for an antibody which facilitates hydrolysis of the inhibitor by thrombin.-Reference-Cited by-同舟云学术

Hydrophobic residues 382-386 of antithrombin III, Ala-Ala-Ala-Ser-Thr, serve as the epitope for an antibody which facilitates hydrolysis of the inhibitor by thrombin.

Published:1990-03 Issue:9 Volume:265 Page:5135-5138
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Asakura S,Hirata H,Okazaki H,Hashimoto-Gotoh T,Matsuda M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference33 articles.

1. The Purification and Mechanism of Action of Human Antithrombin-Heparin Cofactor

2. The covalent nature of the human antithrombin III–thrombin bond

3. The active site of antithrombin. Release of the same proteolytically cleaved form of the inhibitor from complexes with factor IXa, factor Xa, and thrombin.

4. Release of a Two-Chain Form of Antithrombin from the Antithrombin-Thrombin Complex

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1. Probing plasma clearance of the thrombin-antithrombin complex with a monoclonal antibody against the putative serpin-enzyme complex receptor-binding site;European Journal of Biochemistry;2003-09-26

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3. Importance of the Hinge Region between α-Helix F and the Main Part of Serpins, Based upon Identification of the Epitope of Plasminogen Activator Inhibitor Type 1 Neutralizing Antibodies;Journal of Biological Chemistry;2000-03

4. Topology of the Stable Serpin-Protease Complexes Revealed by an Autoantibody That Fails to React with the Monomeric Conformers of Antithrombin;Journal of Biological Chemistry;1999-02

5. Identification of an Epitope in Antithrombin Appearing on Insertion of the Reactive-Bond Loop into the A β-Sheet;Biochemistry;1996-01-01