skip to content
Fundamentals of Enzyme Kinetics. Preview this item
ClosePreview this item

Fundamentals of Enzyme Kinetics.

Author: Athel Cornish-Bowden
Publisher: Elsevier Science, 2014.
Edition/Format:   eBook : Document : EnglishView all editions and formats
Summary:
Fundamentals of Enzyme Kinetics details the rate of reactions catalyzed by different enzymes and the effects of varying the conditions on them. The book includes the basic principles of chemical kinetics, especially the order of a reaction and its rate constraints. The text also gives an introduction to enzyme kinetics - the idea of an enzyme-substrate complex; the Michaelis-Menten equation; the steady state  Read more...
Getting this item's online copy... Getting this item's online copy...

Find a copy in the library

Getting this item's location and availability... Getting this item's location and availability...

WorldCat

Find it in libraries globally
Worldwide libraries own this item

Details

Genre/Form: Electronic books
Additional Physical Format: Erscheint auch als:
Cornish-Bowden, Athel. Fundamentals of Enzyme Kinetics
Druck-Ausgabe
Material Type: Document, Internet resource
Document Type: Internet Resource, Computer File
All Authors / Contributors: Athel Cornish-Bowden
ISBN: 1322334293 9781322334295 9781483161198 1483161196
OCLC Number: 897021983
Description: 1 online resource
Contents: Cover ; Fundamentals of Enzyme Kinetics; Copyright; Table of contents ; Preface; Principal symbols used in this book; Chapter 1. Basic principles of chemical kinetics; 1.1 Order of a reaction; 1.2 Determination of the order of a reaction; 1.3 Dimensions of rate constants; 1.4 Reversible reactions; 1.5 Determination of first-order rate constants; 1.6 Influence of temperature on rate constants; 1.7 Transition-state theory; Problems; Chapter 2. Introduction to enzyme kinetics; 2.1 Early studies: the idea of an enzyme-substrate complex; 2.2 Michaelis-Menten equation; 2.3 Steady-state treatment. 2.4 Validity of the steady-state assumption2.5 Graphical representation of the Michaelis-Menten equation; 2.6 Reversible Michaelis-Menten mechanism; 2.7 Product inhibition; 2.8 Integrated Michaelis-Menten equation; Problems; Chapter 3. Practical considerations; 3.1 Purification of enzymes; 3.2 Enzyme assays; 3.3 Coupled assays; 3.4 Protein determination; 3.5 Presentation of results of a purification; 3.6 Detecting enzyme inactivation; 3.7 Experimental design: choice of substrate concentrations; 3.8 Choice of pH, temperature and other conditions; 3.9 Use of replicate observations. 3.10 Treatment of ionic equilibriaProblems; Chapter 4. How to derive steady-state rate equations; 4.1 King-Altman method; 4.2 Modifications to the King-Altman method; 4.3 Cha's method for reactions containing steps at equilibrium; 4.4 Analysing mechanisms by inspection; Problems; Chapter 5. Inhibitors and activators; 5.1 Reversible and irreversible inhibitors; 5.2 Competitive inhibition; 5.3 Mixed inhibition; 5.4 Uncompetitive inhibition; 5.5 Plotting inhibition results; 5.6 Inhibition by a competing substrate; 5.7 Activation; 5.8 Hyperbolic inhibition and activation. 5.9 Design of inhibition experiments 5.10 Non-productive binding; 5.11 Substrate inhibition; 5.12 Chemical modification as a means of identifying essential groups; Problems; Chapter 6. Two-substrate reactions; 6.1 Introduction; 6.2 Types of mechanism; 6.3 Rate equations; 6.4 Initial-velocity measurements in the absence of products; 6.5 Substrate inhibition; 6.6 Product inhibition; 6.7 Design of experiments; 6.8 Isotope exchange; 6.9 Reactions with three or more substrates; Problems; Chapter 7. Effects of pH and temperature on enzymes; 7.1 pH and enzyme kinetics. 7.2 Acid-base properties of proteins7.3 Ionization of a dibasic acid; 7.4 Effect of pH on enzyme kinetic constants; 7.5 Ionization of the substrate; 7.6 More complex pH effects; 7.7 Temperature dependence of enzyme-catalysed reactions; Problems; Chapter 8. Control of enzyme activity; 8.1 Necessity for metabolic control; 8.2 Binding of oxygen to haemoglobin; 8.3 Hill equation; 8.4 Adair equation; 8.5 Definition of co-operativity; 8.6 Induced fit; 8.7 Symmetry model of Monod, Wyman and Changeux; 8.8 Sequential model of Koshland, Némethy and Filmer.

Abstract:

Fundamentals of Enzyme Kinetics details the rate of reactions catalyzed by different enzymes and the effects of varying the conditions on them. The book includes the basic principles of chemical kinetics, especially the order of a reaction and its rate constraints. The text also gives an introduction to enzyme kinetics - the idea of an enzyme-substrate complex; the Michaelis-Menten equation; the steady state treatment; and the validity of its assumption. Practical considerations, the derivation of steady-state rate equations, inhibitors and activators, and two-substrate reactions are also.
Retrieving notes about this item Retrieving notes about this item

Reviews

User-contributed reviews

Tags

Be the first.
Confirm this request

You may have already requested this item. Please select Ok if you would like to proceed with this request anyway.

Close Window

Please sign in to WorldCat 

Don't have an account? You can easily create a free account.