Fundamentals of enzyme kinetics. (©2012)

• Record Type: Book
• Further Information: Note: Athel Cornish-Bowden.
• Other Names: Cornish-Bowden, Athel
• Contents: Title Page; Contents; 1 Basic Principles of Chemical Kinetics; 1.1 Symbols, terminology and abbreviations; 1.2 Order of a reaction; 1.2.1 Order and molecularity; 1.2.2 First-order kinetics; 1.2.3 Second-order kinetics; 1.2.4 Third-order kinetics; 1.2.5 Zero-order kinetics; 1.2.6 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; 1.7 Catalysis; 1.8 The influence of temperature and pressure on rate constants; 1.8.1 The Arrhenius equation; 1.8.2 Elementary collision theory 1.8.3 Transition-state theory1.8.4 Effects of hydrostatic pressure; Chapter summary; Problems; 2 Introduction to Enzyme Kinetics; 2.1 The idea of an enzyme-substrate complex; 2.2 The Michaelis-Menten equation; 2.3 The steady state of an enzyme-catalyzed reaction; 2.3.1 The Briggs-Haldane treatment; 2.3.2 Parameters of the Michaelis-Menten equation; 2.3.3 Units of enzyme activity; 2.3.4 The curve defined by the Michaelis-Menten equation; 2.3.5 Mutual depletion kinetics; 2.3.6 Ways of writing the Michaelis-Menten equation; 2.4 Specificity; 2.4.1 The fundamental property of enzymes 2.4.2 Discrimination between mixed substrates2.4.3 Comparing different catalysts; 2.5 Validity of the steady-state assumption; 2.6 Graphs of the Michaelis-Menten equation; 2.6.1 Plotting v against a; 2.6.2 The double-reciprocal plot; 2.6.3 The plot of a/v against a; 2.6.4 The plot of v against v/a; 2.6.5 Origins of the plots; 2.6.6 The direct linear plot; 2.7 The reversible Michaelis-Menten mechanism; 2.7.1 The reversible rate equation; 2.7.2 The Haldane relationship; 2.7.3 "One-way enzymes"; 2.8 Product inhibition; 2.9 Integration of enzyme rate equations 2.9.1 Michaelis-Menten equation without product inhibition2.9.2 Effect of product inhibition on progress curves; 2.9.3 Other problems with time courses; 2.9.4 Characterizing mutant enzymes; 2.9.5 Accurate estimation of initial rates; 2.9.6 Time courses for other mechanisms; Chapter summary; Problems; 3 "Alternative" enzymes; 3.1 Introduction; 3.2 Artificial enzymes; 3.3 Site-directed mutagenesis; 3.4 Chemical mimics of enzyme catalysis; 3.5 Catalytic RNA; 3.6 Catalytic antibodies; Chapter summary; Problems; 4 Practical Aspects of Kinetics; 4.1 Enzyme assays 4.1.1 Discontinuous and continuous assays4.1.2 Estimating the initial rate; 4.1.3 Increasing the straightness of the progress curve; 4.1.4 Coupled assays; 4.2 Detecting enzyme inactivation; 4.3 Experimental design; 4.3.1 Choice of substrate concentrations; 4.3.2 Choice of pH, temperature and other conditions; 4.3.3 Use of replicate observations; 4.4 Treatment of ionic equilibria; Chapter summary; Problems; 5 Deriving Steady-state Rate Equations; 5.1 Introduction; 5.2 The principle of the King-Altman method; 5.3 The method of King and Altman; 5.4 The method of Wong and Hanes
• Edition: 4th completely rev. and greatly enl. ed
• Publisher Details: Weinheim : Wiley-VCH
• Publication Date: 2012
• Copyright Date: 2012
• Extent: 1 online resource (xviii, 498 pages), illustrations
• Subjects: 572.744; Enzyme kinetics; Chemical kinetics; Kinetics; SCIENCE -- Life Sciences -- Biochemistry; Chemical kinetics; Enzyme kinetics; Electronic books
• Languages: English
• ISBNs: 9783527665488; 9783527665495; 3527665498
• Related ISBNs: 352766548X; 9783527330744; 3527330747
• Notes: Note: Includes bibliographical references and index.; Note: Print version record.
• Access Rights: Legal Deposit; Only available on premises controlled by the deposit library and to one user at any one time; The Legal Deposit Libraries (Non-Print Works) Regulations (UK).
• Access Usage: Restricted: Printing from this resource is governed by The Legal Deposit Libraries (Non-Print Works) Regulations (UK) and UK copyright law currently in force.