Enzyme Kinetics : Principles and Methods
Hans. Bisswanger
Bok Engelsk 2008 · Electronic books.
Annen tittel | |
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Utgitt | Hoboken : : Wiley, , 2008.
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Omfang | 1 online resource (321 p.)
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Utgave | 2nd ed.
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Opplysninger | Description based upon print version of record.. - Enzyme Kinetics; Preface to the Second English Edition; Preface to the First English Edition; Contents; Symbols and Abbreviations; Introduction and Definitions; References; 1 Multiple Equilibria; 1.1 Diffusion; 1.2 Interaction between Macromolecules and Ligands; 1.2.1 Binding Constants; 1.2.2 Macromolecules with One Binding Site; 1.3 Macromolecules with Identical Independent Binding Sites; 1.3.1 General Binding Equation; 1.3.2 Graphic Representations of the Binding Equation; 1.3.2.1 Direct and Linear Diagrams; 1.3.2.2 Analysis of Binding Data from Spectroscopic Titrations. - 1.3.3 Binding of Different Ligands, Competition1.3.4 Non-competitive Binding; 1.4 Macromolecules with Non-identical, Independent Binding Sites; 1.5 Macromolecules with Identical, Interacting Binding Sites, Cooperativity; 1.5.1 The Hill Equation; 1.5.2 The Adair Equation; 1.5.3 The Pauling Model; 1.5.4 Allosteric Enzymes; 1.5.5 The Symmetry or Concerted Model; 1.5.6 The Sequential Model and Negative Cooperativity; 1.5.7 Analysis of Cooperativity; 1.5.8 Physiological Aspects of Cooperativity; 1.5.9 Examples of Allosteric Enzymes; 1.5.9.1 Hemoglobin; 1.5.9.2 Aspartate Transcarbamoylase. - 1.5.9.3 Aspartokinase1.5.9.4 Phosphofructokinase; 1.5.9.5 Allosteric Regulation of the Glycogen Metabolism; 1.5.9.6 Membrane Bound Enzymes and Receptors; 1.6 Non-identical, Interacting Binding Sites; References; 2 Enzyme Kinetics; 2.1 Reaction Order; 2.1.1 First Order Reactions; 2.1.2 Second Order Reactions; 2.1.3 Zero Order Reactions; 2.2 Steady-State Kinetics and the Michaelis-Menten Equation; 2.2.1 Derivation of the Michaelis-Menten Equation; 2.3 Analysis of Enzyme Kinetic Data; 2.3.1 Graphical Representations of the Michaelis-Menten Equation. - 2.3.1.1 Direct and Semi-logarithmic Representations2.3.1.2 Direct Linear Plots; 2.3.1.3 Linearization Methods; 2.3.2 Analysis of Progress Curves; 2.3.2.1 Integrated Michaelis-Menten Equation; 2.3.2.2 Determination of Reaction Rates; 2.3.2.3 Graphic Methods for Rate Determination; 2.3.2.4 Graphic Determination of True Initial Rates; 2.4 Reversible Enzyme Reactions; 2.4.1 Rate Equation for Reversible Enzyme Reactions; 2.4.2 The Haldane Relationship; 2.4.3 Product Inhibition; 2.5 Enzyme Inhibition; 2.5.1 Unspecific Enzyme Inhibition; 2.5.2 Irreversible Enzyme Inhibition. - 2.5.2.1 General Features of Irreversible Enzyme Inhibition2.5.2.2 Suicide Substrates; 2.5.2.3 Transition State Analogs; 2.5.2.4 Analysis of Irreversible Inhibitions; 2.5.3 Reversible Enzyme Inhibition; 2.5.3.1 General Rate Equation; 2.5.3.2 Non-Competitive Inhibition and Graphic Representation of Inhibition Data; 2.5.3.3 Competitive Inhibition; 2.5.3.4 Uncompetitive Inhibition; 2.5.3.5 Partially Non-competitive Inhibition; 2.5.3.6 Partially Uncompetitive Inhibition; 2.5.3.7 Partially Competitive Inhibition; 2.5.3.8 Noncompetitive and Uncompetitive Product Inhibition. - 2.5.3.9 Substrate Inhibition. - This new, expanded and updated edition of the user-friendly and comprehensive treatise on enzyme kinetics expertly balances theory and practice. This is an indispensable aid for advanced students and professionals working with enzymes, whether biochemists, biotechnologists, chemical biologists, pharmacologists or bioengineers in academia, industry and clinical research.
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Emner | |
Sjanger | |
Dewey | |
ISBN | 9783527319572
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