Enzyme Kinetics

Principles and Methods

Bisswanger, Hans

3. Edition August 2017
XX, 316 Pages, Hardcover
10 tables
Handbook/Reference Book

ISBN: 978-3-527-34251-8

Wiley-VCH, Weinheim

Wiley Online Library Content Sample Chapter Index

Short Description

The author's integrated approach to the theoretical and methodological aspects of enzyme kinetics makes this a highly useful tool for understanding, measuring and modeling enzyme action as well as an excellent introduction to the field.

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Further versions

Now in full color for a more intuitive learning experience, this new edition of the long-selling reference also features a number of new developments in methodology and the application of enzyme kinetics.
Starting with a description of ligand binding equilibria, the experienced author goes on to discuss simple and complex enzyme reactions in kinetic terms. Special cases such as membrane-bound and immobilized enzymes are considered, as is the influence of external conditions, such as temperature and pH value. The final part of the book then covers a range of widely used measurement methods and compares their performance and scope of application.
With its unique mix of theory and practical advice, this is an invaluable aid for teaching as well as for experimental work.

PART I: Ligand Binding
Diffusion
Interaction between macromolecules and ligands
Identical independent binding sites
Non-identical independent binding sites
Identical interacting binding sites, cooperativity
Non-identical interacting binding sites

PART II: Enzyme Kinetics
Reaction Order
Steady-state kinetics and the Michaelis-Menten Equation
Reversible enzyme reactions
Enzyme inhibition
Multi-substrate reactions
Rate equations of complex enzyme mechanisms
Allosteric enzymes
pH and temperature dependence
Isotope exchange kinetics and isotope effects
Ribozymes
Enyzmes with polymeric substrates
Immobilized enzymes
Kinetics of transport processes
Enzyme reactions at membrane interfaces

PART III: Methods
Methods for investigating multiple equilibria
Electrochemical methods
Calorimetry
Spectroscopic methods
Measurement of fast reactions

Hans Bisswanger was Professor at the Interfaculty Institute of Biochemistry at the University of Tübingen (Germany), where he has developed and taught for many years an intensive course on enzyme kinetics, enzyme technology and ligand binding. His scientific interest lies with structural and regulatory mechanisms of multi-enzyme complexes, thermophilic enzymes and the technical application of immobilized enzymes. He is the author of two well-known books on enzymology that have appeared in different languages and editions.

H. Bisswanger, University of Tübingen, Germany