The Chemical Biology of Thrombin
Auteur : Lundblad Roger L.
This book is a comprehensive review of thrombin, especially as regulatory protease. The ready availability of highly purified thrombin has stimulated rapid advances in the cell biology of this important macromolecule. The text focuses on research findings from the discovery of thrombin by Andrew Buchanan in 1842 to the present. A substantial amount of this work was conducted by the author and his colleagues. His work on the purification of thrombin was seminal to much subsequent work on thrombin. This volume provides a framework for future studies now made possible by the discovery of the importance of exosites in the physiology of thrombin function. The current work describes the process of the development of an oral inhibitor of thrombin used in the prevention of thrombosis.
Key Features
- Reviews the history of Thrombin (Fibrin Ferment)
- Documents the relation of protein engineering and chemical modification in the study of thrombin
- Summarizes the interaction of thrombin with fibrinogen and fibrin
- Outlines the role of exosites in thrombin function
- Describes the development of an oral inhibitor for thrombin
Preface. Acknowledgements. About the Author. The History of Thrombin. The Formation of Thrombin. Structural Biology of Thrombin. The Use of Protein Engineering (Mutagenesis) to Study Functional Regions in Thrombin Expression and Characterization of Recombinant Thrombins. Chemical Modification of Thrombin. The Interaction of Thrombin with Fibrinogen and Fibrin.Thrombin and Platelets. Inhibitors of Thrombin. Index.
Roger L. Lundblad is an independent consultant based in Chapel Hill, North Carolina. He is also an adjunct professor of pathology at the University of North Carolina, Chapel Hill.
Date de parution : 05-2022
15.6x23.4 cm
Date de parution : 01-2024
15.6x23.4 cm
Thèmes de The Chemical Biology of Thrombin :
Mots-clés :
Protein Structure & Function; Blood Clotting and Coagulation Mechanisms; Hemostasis; Proteolysis; DAPA; Bind Thrombin; Fibrin Clot; Fibrinogen Clotting; Bovine Thrombin; Thrombin Function; Ethacridine Lactate; Trisodium Citrate; Thrombin Inhibitor; Heparin Cofactor Ii; Active Site Serine; 60s Loop; Active Site Histidine; Mouse Platelets; High Thrombin Concentrations; Diphenyl Sulfones; Factor Xa; Prothrombinase Complex; Par Protein; Specific Chemical Modification; Peptide Chloromethyl Ketones; Alanine Scanning; Platelet Activation; Histidine Rich Glycoprotein; Prothrombin Complex Concentrates