Kinetic studies of enzyme action provide powerful insights into the underlying mechanisms of catalysis and regulation. These approaches are equally useful in examining the action of newly discovered enzymes and therapeutic agents.
Contemporary Enzyme Kinetics and Mechanism, Second Edition presents key articles from Volumes 63, 64, 87, and 249 ofMethods in Enzymology. The chapters describe the most essential and widely applied strategies. A set of exercises and problems is included to facilitate mastery of these topics.
The book will aid the reader to design, execute, and analyze kinetic experiments on enzymes. Its emphasis on enzyme inhibition will also make it attractive to pharmacologists and pharmaceutical chemists interested in rational drug design.
Of the seventeen chapters presented in this new edition, ten did not previously appear in the first edition.
Key Features
* Transient kinetic approaches to enzyme mechanisms
* Designing initial rate enzyme assay
* Deriving initial velocity and isotope exchange rate equations
* Plotting and statistical methods for analyzing rate data
* Cooperativity in enzyme function
* Reversible enzyme inhibitors as mechanistic probes
* Transition-state and multisubstrate inhibitors
* Affinity labeling to probe enzyme structure and function
* Mechanism-based enzyme inactivators
* Isotope exchange methods for elucidating enzymatic catalysis
* Kinetic isotope effects in enzyme catalysis
* Site-directed mutagenesis in studies of enzyme catalysis
Le informazioni nella sezione "Riassunto" possono far riferimento a edizioni diverse di questo titolo.
Daniel Lee Purich has been at the forefront of biochemistry research for more than 25 years. He was awarded the National Institutes of Health Research Career Development Award from 1977–1982, the Plous Teaching Award (the University of California Santa Barbara Campus-Wide Teaching Award) in 1977, has been a member of the National Institutes of Health Biochemistry Study Section from 1982–1985, and a member of the Journal of Biological Chemistry Editorial Board from 1981–1986. He has been a member of the American Society of Biological Chemists, the American Chemical Society, the New York Academy of Sciences, the Biochemical Society, and the American Society for Cell Biology. Dr. Purich is currently a Professor and Chairman of the Department of Biochemistry and Molecular Biology at the Florida College of Medicine. He is the author and editor of numerous scientific publications.
Kinetic studies of enzyme action provide powerful insights into the underlying mechanisms of catalysis and regulation. These approaches are equally useful in examining the action of newly discovered enzymes and therapeutic agents.
Contemporary Enzyme Kinetics and Mechanism, Second Edition presents key articles from Volumes 63, 64, 87, and 249 of Methods in Enzymology. The chapters describe the most essential and widely applied strategies. A set of exercises and problems is included to facilitate mastery of these topics.
Key Features
* Transient kinetic approaches to enzyme mechanisms
* Designing initial rate enzyme assay
* Deriving initial velocity and isotope exchange rate equations
* Plotting and statistical methods for analyzing rate data
* Cooperativity in enzyme function
* Reversible enzyme inhibitors as mechanistic probes
* Transition-state and multisubstrate inhibitors
* Affinity labeling to probe enzyme structure and function
* Mechanism-based enzyme inactivators
* Isotope exchange methods for elucidating enzymatic catalysis
* Kinetic isotope effects in enzyme catalysis
* Site-directed mutagenesis in studies of enzyme catalysis|Kinetic studies of enzyme action provide powerful insights into the underlying mechanisms of catalysis and regulation. These approaches are equally useful in examining the action of newly discovered enzymes and therapeutic agents.
Contemporary Enzyme Kinetics and Mechanism, Second Edition presents key articles from Volumes 63, 64, 87, and 249 ofMethods in Enzymology. The chapters describe the most essential and widely applied strategies. A set of exercises and problems is included to facilitate mastery of these topics.
Key Features
* Transient kinetic approaches to enzyme mechanisms
* Designing initial rate enzyme assay
* Deriving initial velocity and isotope exchange rate equations
* Plotting and statistical methods for analyzing rate data
* Cooperativity in enzyme function
* Reversible enzyme inhibitors as mechanistic probes
* Transition-state and multisubstrate inhibitors
* Affinity labeling to probe enzyme structure and function
* Mechanism-based enzyme inactivators
* Isotope exchange methods for elucidating enzymatic catalysis
* Kinetic isotope effects in enzyme catalysis
* Site-directed mutagenesis in studies of enzyme catalysis
Le informazioni nella sezione "Su questo libro" possono far riferimento a edizioni diverse di questo titolo.
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