omitir hasta el contenido
Fundamentals of Enzyme Kinetics. Ver este material de antemano
CerrarVer este material de antemano

Fundamentals of Enzyme Kinetics.

Autor: Athel Cornish-Bowden
Editorial: Elsevier Science, 2014.
Edición/Formato:   Libro-e : Documento : Inglés (eng)Ver todas las ediciones y todos los formatos
Resumen:
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  Leer más
Consiguiendo una copia en línea de este material… Consiguiendo una copia en línea de este material…

Encontrar un ejemplar en la biblioteca

Obtener la ubicación y disponibilidad de este material… Obtener la ubicación y disponibilidad de este material…

WorldCat

Encontrarlo en una biblioteca por todo el mundo
Bibliotecas por todo el mundo tienen este material

Detalles

Género/Forma: Electronic books
Formato físico adicional: Erscheint auch als:
Cornish-Bowden, Athel. Fundamentals of Enzyme Kinetics
Druck-Ausgabe
Tipo de material: Documento, Recurso en Internet
Tipo de documento Recurso internet, Archivo de computadora
Todos autores / colaboradores: Athel Cornish-Bowden
ISBN: 1322334293 9781322334295 9781483161198 1483161196
Número OCLC: 897021983
Descripción: 1 online resource
Contenido: 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.

Resumen:

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.
Recuperando notas sobre este material Recuperando notas sobre este material

Reseñas

Reseñas contribuidas por usuarios

Etiquetas

Ser el primero.
Confirmar este pedido

Ya ha pedido este material. Escoja OK si desea procesar el pedido de todos modos.

Cerrar ventana

Inicie una sesión con WorldCat 

¿No tienes una cuenta? Puede fácilmente crear una cuenta gratuita.