Contemporary Enzyme Kinetics and Mechanism
Selected Methods in Enzymology
2nd Edition
Published on 21. August 1996
Book
Paperback/Softback
541 pages
978-0-12-568052-3 (ISBN)
Description
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.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.
More details
Series
Edition
2nd edition
Language
English
Place of publication
San Diego
United States
Publishing group
Elsevier Science Publishing Co Inc
Target group
Professional and scholarly
Students and professionals in biochemistry, biophysics, molecular biology, pharmacology, and pharmaceutical chemistry.
Edition type
New edition
Dimensions
Height: 229 mm
Width: 152 mm
Weight
820 gr
ISBN-13
978-0-12-568052-3 (9780125680523)
Copyright in bibliographic data and cover images is held by Nielsen Book Services Limited or by the publishers or by their respective licensors: all rights reserved.
Schweitzer Classification
Other editions
New editions
Book
11/2009
3rd Edition
Academic Press
€77.00
Shipment within 15-20 days
Person
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.
Content
C.A. Fierke and G.G. Hammes, Transient Kinetic Approaches to Enzyme Mechanisms.
R.D. Allison and D.L. Purich, Practical Considerations in the Design of Initial Velocity Enzyme Assays.
C.Y. Huang, Derivation ofInitial Velocity and Isotope Exchange Rate Equations.
F.B. Rudolph and H.J. Fromm, Plotting Methods for Analyzing Enzyme Rate Data.
B. Mannervik, Regression Analysis, Experimental Error, and Statistical Criteria in the Design and Analysis of Experiments for Discrimination between Rival Kinetic Models.
K.E. Neet, Cooperactivity in Enzyme Function: Equilibrium and Kinetic Aspects.
B.F. Cooper and F.B. Rudolph, Product Inhibition Applications.
H.J. Fromm, Reversible Enzyme Inhibitors as Mechanistic Probes.
A. Radzicka and R. Wolfenden, Transition State and Multisubstrate Analog Inhibitors.
B.V. Plapp, Application of Affinity Labeling for Studying Structure and Function of Enzymes.
R.B. Silverman, Mechanism-Based Enzyme Inactivators.
D.L. Purich and R.D. Allison, Isotope Exchange Methods for Elucidating Enzymic Catalysis.
L.S. Mullins and F.M. Raushel, Positional Isotope Exchange as a Probe of Enzyme Action.
W.W. Cleland, Isotope Effects: Determination of Enzyme Transition State Structure.
B.J. Bahnson and J.P. Klinman, Hydrogen Tunneling in Enzyme Catalysis.
B.V. Plapp, Site-Directed Mutagenesis: A Tool for Studying Enzyme Catalysis.
D.L. Purich, Selected Exercises and Problems in Modern Enzyme Dynamics.
R.D. Allison and D.L. Purich, Practical Considerations in the Design of Initial Velocity Enzyme Assays.
C.Y. Huang, Derivation ofInitial Velocity and Isotope Exchange Rate Equations.
F.B. Rudolph and H.J. Fromm, Plotting Methods for Analyzing Enzyme Rate Data.
B. Mannervik, Regression Analysis, Experimental Error, and Statistical Criteria in the Design and Analysis of Experiments for Discrimination between Rival Kinetic Models.
K.E. Neet, Cooperactivity in Enzyme Function: Equilibrium and Kinetic Aspects.
B.F. Cooper and F.B. Rudolph, Product Inhibition Applications.
H.J. Fromm, Reversible Enzyme Inhibitors as Mechanistic Probes.
A. Radzicka and R. Wolfenden, Transition State and Multisubstrate Analog Inhibitors.
B.V. Plapp, Application of Affinity Labeling for Studying Structure and Function of Enzymes.
R.B. Silverman, Mechanism-Based Enzyme Inactivators.
D.L. Purich and R.D. Allison, Isotope Exchange Methods for Elucidating Enzymic Catalysis.
L.S. Mullins and F.M. Raushel, Positional Isotope Exchange as a Probe of Enzyme Action.
W.W. Cleland, Isotope Effects: Determination of Enzyme Transition State Structure.
B.J. Bahnson and J.P. Klinman, Hydrogen Tunneling in Enzyme Catalysis.
B.V. Plapp, Site-Directed Mutagenesis: A Tool for Studying Enzyme Catalysis.
D.L. Purich, Selected Exercises and Problems in Modern Enzyme Dynamics.