Thrombin

1. Front Matter

   Pages i-xvi

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2. Structure

   1. Front Matter

      Pages 1-1

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   2. X-Ray Crystal Structures of Human α-Thrombin and of the Human Thrombin-Hirudin Complex

      • Wolfram Bode, Robert Huber, Timothy J. Rydel, Alexander Tulinsky

      Pages 3-61

   3. Nuclear Magnetic Resonance Studies of Thrombin-Fibrinopeptide and Thrombin-Hirudin Complexes

      • Feng Ni, Kenneth D. Gibson, Harold A. Scheraga

      Pages 63-85

   4. ESR and Fluorescence Studies of Thrombin Active Site Conformation

      • Lawrence J. Berliner

      Pages 87-113

3. Biochemistry

   1. Front Matter

      Pages 115-115

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   2. Synthetic Substrates and Inhibitors of Thrombin

      • James C. Powers, Chih-Min Kam

      Pages 117-158

   3. Regulation of Thrombin by Antithrombin and Heparin Cofactor II

      • Steven T. Olson, Ingemar Björk

      Pages 159-217

   4. Hirudin Interactions with Thrombin

      • Stuart R. Stone, John M. Maraganore

      Pages 219-256

   5. Activation of Human Plasma Factor XIII by Thrombin

      • L. Lorand, J. T. Radek

      Pages 257-271

4. Physiology

   1. Front Matter

      Pages 273-273

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   2. Effect of Chemical Modification of α-Thrombin on Its Reaction with Platelets and Nucleated Cells

      • Nicholas J. Greco

      Pages 275-314

   3. Functional Domains in Thrombin Outside the Catalytic Site

      • Rachel Bar-Shavit, Miriam Benezra, Valerie Sabbah, Elisabetta Dejana, Israel Vlodavsky, George D. Wilner

      Pages 315-350

   4. Postclotting Cellular Effects of Thrombin Mediated by Interaction with High-Affinity Thrombin Receptors

      • Darrell H. Carney

      Pages 351-396

   5. Regulation of Thrombin-Induced Endothelial Barrier Dysfunction and Prostaglandin Synthesis

      • Joe G. N. Garcia, Judy L. Aschner, Asrar B. Malik

      Pages 397-430

5. Back Matter

   Pages 431-438

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Research on thrombin structure and function has progressed significantly over the past three decades. We are continually discovering new functions f()r this enzyme in biology. Yet, until quite recently, a full, detailed, three­ dimensional picture of its structure was difficult to attain. We believe that this text represents a turning point and, more appropriately, a new start­ ing point for thrombin studies. Our goal for this text is to present a thorough and rounded-out coverage of thrombin chemistry and biochem­ istry in order to provide the biochemist and physiologist with an excellent desk reference on almost any thrombin-related problem. This volume is organized into three general thrombin topic areas: Structure, Biochemistry, and Physiology. In Part 1, Structure, we open with the complete three-dimensional x-ray structures of two inhibited human thrombin complexes, one of which is the thrombin-hirudin com­ plex. These complexes are also addressed in the chapter on structural studies in solution, which include NMR, ESR, and fluorescence. Part 2, Biochemistry, includes chapters on synthetic thrombin inhibitors, protein inhibitors (e.g., antithrombin III, hirudin), and thrombin interactions with factor XIII. Part 3, Physiology, covers such topics as chemotactic activities, interactions with cell surfaces, and the vascular endothelium.

• Peptide
• X-ray
• biochemistry
• endothelium
• magnetic resonance
• physiology

• The Ohio State University, Columbus, USA

  Lawrence J. Berliner

Dr. Lawrence J. Berliner is currently Professor and Chair of the Department of Chemistry and Biochemistry at the University of Denver after retiring from Ohio State University, where he spent a 32-year career in the area of biological magnetic resonance (EPR and NMR). He is the Series Editor for Biological Magnetic Resonance, which he launched in 1979.

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