Kinetics of the inhibition of thrombin by hirudin.
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Summary
The dissociation constant for hirudin was determined by varying the concentration of hirUDin in the presence of a fixed concentration of thrombin and tripeptidyl p-nitroanilide substrate and was markedly dependent on the ionic strength of the assay.
- Type
- article
- Published
- 1986-08-12
- Cited by
- 570
- References
- 23
- OpenAlex
- https://openalex.org/W2013547341
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:23993374
Keywords
Ionic strength, Hirudin, Dissociation constant, Chemistry, Dissociation (chemistry)
References
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Cited by
- The effect of substituting phosphotyrosine for sulphotyrosine on the activity of hirudin.
- Mechanism of the inhibition of alpha-thrombin by hirudin-derived fragments hirudin(1-47) and hirudin(45-65).
- Interaction between chicken cystatin and the cysteine proteinases actinidin, chymopapain A, and ficin.
- Analysis of the secondary structure of hirudin and the mechanism of its interaction with thrombin.
- Identification of regions of alpha-thrombin involved in its interaction with hirudin.
- Proteinase Inhibitors from the Medicinal Leech Hirudo medicinalis
- Comparative studies on the inhibitory spectrum of recombinant hirudin, DuP 714 and heparin on thrombin and factor Xa generation in biochemically defined systems.
- Rapid inhibition of the sperm protease acrosin by protein C inhibitor.
- Recombinant Hirudin in the Prevention of Venous Thromboembolism in Patients Undergoing Elective Hip Surgery
- New anticoagulant drugs.
- Tyrosine O‐sulfation promotes proteolytic processing of progastrin.
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- Cardiovascular pharmacology: new drugs and new indications.
- Phage display as a powerful tool to engineer protease inhibitors.
- Batroxobin Binds Fibrin with Higher Affinity and Promotes Clot Expansion to a Greater Extent than Thrombin*
- Evolution of Serpin Specificity: Cooperative Interactions in the Reactive-Site Loop Sequence of Antithrombin Specifically Restrict the Inhibition of Activated Protein C
- Hirudin: Its biology and clinical use
- Thrombin inhibition by synthetic hirudin peptides.
- Molecular basis for the inhibition of thrombin by hirudin.
- Novel Allosteric Inhibitors of Thrombin
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