Study of Enzymes: Enzyme Catalysts, Kinetics, and Substrate Binding [Kõva köide]

(University of Utah)
  • Formaat: Hardback, 488 pages, kõrgus x laius: 254x178 mm, kaal: 1061 g, 1 Halftones, black and white; 41 Tables, black and white
  • Sari: Routledge Revivals 1
  • Ilmumisaeg: 30-Jun-2020
  • Kirjastus: CRC Press
  • ISBN-10: 0367261197
  • ISBN-13: 9780367261191
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  • Formaat: Hardback, 488 pages, kõrgus x laius: 254x178 mm, kaal: 1061 g, 1 Halftones, black and white; 41 Tables, black and white
  • Sari: Routledge Revivals 1
  • Ilmumisaeg: 30-Jun-2020
  • Kirjastus: CRC Press
  • ISBN-10: 0367261197
  • ISBN-13: 9780367261191
Teised raamatud teemal:
First published in 1990, this comprehensive monograph consists of two parts: Volume I, entitled Enzyme Catalysis, Kinetics, and Substrate Binding; and Volume II, entitled Mechanism of Enzyme Action. Volume I focuses on several aspects of enzyme catalytic behavior, their steady-state and transient-state kinetics, and the thermodynamic properties of substrate binding. Packed with figures, tables, schemes, and photographs, this volume contains over 1,000 references, including references regarding enzymology's fascinating history. This comprehensive book is of particular interest to enzymology students, teachers, and researchers.
Volume II presents selected "cutting edge" examples of techniques and approaches being pursued in biochemistry. This up-to-date resource includes 11 chapters, which illustrate important theoretical and practical aspects of enzyme mechanisms. It also features selected examples in which today's most important techniques, ideas, and theories are used to elaborate on the intricate nature of enzyme action mechanisms. This particular volume provides important information for both the novice and the seasoned investigator.
Enzyme Catalysis and Steady-State Kinetics: Historical Introduction, Theories of Enzyme Catalysis, and Some Elementary Considerations of Enzyme Kinetics. A Description of Steady-State Kinetics and Quasi- or Rapid Equilibrium Kinetics by a Development of the Rate Expressions for Several Selected Mechanisms and Their Characteristics. Inhibition and Product Inhibition. Effects of pH and Temperature. Effect of Metal Cofactors on the Reaction Velocity. Enzyme Kinetics and Substrate Binding: Some Remarks on Isotope Exchange Studies and Kinetic Isotope Effects. Non-Michaelis-Menten Kinetics and Allosteric Kinetics. Equilibrium Ligand Binding-Multiple Equilibria. Some Complex Kinetic Mechanisms and Treatment of Enzyme Kinetic Data. Kinetics of the Transient Phase or Pre-Steady-State Phase of Enzyme Reactions. Appendix
1. Appendix
2. References. Index.
Stephen A. Kuby, Ph.D., is a Professor of Biochemistry and Research Professor of Medicine at the University of Utah School of Medicine, Salt Lake City, Utah. He is also the head of the Biochemical Division of the Laboratory for the Study of Hereditary and Metabolic Disorders, University of Utah Research Park, Salt Lake City, Utah 84108. He graduated SummacumLaude from New York University in 1948 with an A.B. in Chemistry. He obtained his M.S. in Biochemistry in 1951, and his Ph.D. in Biochemistry in 1953 at the University of Wisconsin under Professor H. A. Lardy. As a recipient of the U.S. Public Health Service Fellowship, he spent his post-doctorate period with Professor B. Chance at the University of Pennsylvania (Johnson Foundation for Medical Physics) and with Professor H. Theorell at the Karolinska Institute (Medical Nobel Institute, Stockholm, Sweden). Following a period at the Enzyme Institute (University of Wisconsin) as an Assistant Professor, in 1963 he joined the faculty at the University of Utah, and has held his present positions since 1969. His research interests have dealt with many aspects of enzyme and protein chemistry and certain aspects of medicinal chemistry and inherited disorders (including the muscular dystrophies). Mechanistic enzymology is his current interest, and "state of the art" approaches are being applied to study of enzyme action, e.g., of the kinases.

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