The COOH-terminal domain of hirudin. An exosite-directed competitive inhibitor of the action of alpha-thrombin on fibrinogen.
Open Access
- 1 August 1990
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 265 (23) , 13484-13489
- https://doi.org/10.1016/s0021-9258(18)77372-9
Abstract
No abstract availableThis publication has 45 references indexed in Scilit:
- Thrombin Anion‐binding Exosite Interactions with Heparin and Various PolyanionsaAnnals of the New York Academy of Sciences, 1989
- Anion-binding exosite of human .alpha.-thrombin and fibrin(ogen) recognitionBiochemistry, 1988
- Enzymic properties of proteolytic derivatives of human .alpha.-thrombinBiochemistry, 1988
- Catalytic competence of human .alpha.- and .gamma.-thrombin in the activation of fibrinogen and factor XIIIBiochemistry, 1987
- Effect of heparin on the interaction between thrombin and hirudinEuropean Journal of Biochemistry, 1987
- Identification of regions of .alpha.-thrombin involved in its interaction with hirudinBiochemistry, 1987
- Multiple complexes of thrombin and heparinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Human .alpha.-thrombin binding to nonpolymerized fibrin-sepharose: evidence for an anionic binding regionBiochemistry, 1985
- Solution composition dependent variation in extinction coefficients for p-NitroanilineBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Slow, spontaneous dissociation of the antithrombin—thrombin complex produces a proteolytically modified form of the inhibitorFEBS Letters, 1980