1;Cover;1 2;Title Page;5 3;Copyright;6 4;Contents;7 5;Preface;13 6;Symbols and Abbreviations;15 7;Introduction and Definitions;17 8;Chapter 1 Multiple Equilibria, Principles, and Derivations;23 8.1;1.1 General Considerations;23 8.2;1.2 Diffusion;24 8.3;1.3 Modes of Ligand Binding;26 8.4;1.4 Interaction between Macromolecules and Ligands;28 8.4.1;1.4.1 Binding Constants;28 8.4.2;1.4.2 Binding to a Single Site;29 8.5;1.5 Binding to Identical Independent Sites;29 8.5.1;1.5.1 General Binding Equation;29 8.5.2;1.5.2 Graphic Representations of the Binding Equation;35 8.5.2.1;1.5.2.1 Direct and Linear Diagrams;35 8.5.2.2;1.5.2.2 Analysis of Binding Data from Spectroscopic Titrations;37 8.5.3;1.5.3 Binding of Different Ligands, Competition;40 8.5.4;1.5.4 Noncompetitive Binding;43 8.6;1.6 Binding to Nonidentical, Independent Sites;45 8.7;References;47 9;Chapter 2 Cooperativity and Allosteric Enzymes;49 9.1;2.1 Binding to Interacting Sites;49 9.1.1;2.1.1 The Hill Equation;49 9.1.2;2.1.2 The Adair Equation;51 9.1.3;2.1.3 The Pauling Model;54 9.2;2.2 Allosteric Enzymes;54 9.2.1;2.2.1 The Symmetry or Concerted Model;55 9.2.2;2.2.2 The Sequential Model and Negative Cooperativity;60 9.2.3;2.2.3 Analysis of Cooperativity;64 9.2.4;2.2.4 Physiological Aspects of Cooperativity;66 9.2.5;2.2.5 Examples of Allosteric Enzymes;68 9.2.5.1;2.2.5.1 Hemoglobin;68 9.2.5.2;2.2.5.2 Aspartate Transcarbamoylase;70 9.2.5.3;2.2.5.3 Aspartokinase;71 9.2.5.4;2.2.5.4 Phosphofructokinase;72 9.2.5.5;2.2.5.5 Allosteric Regulation of the Glycogen Metabolism;72 9.2.5.6;2.2.5.6 Membrane-Bound Enzymes and Receptors;72 9.3;2.3 Binding to Nonidentical, Interacting Sites;73 9.4;References;74 10;Chapter 3 From Reaction Order to the Michaelis-Menten Law: Fundamental Relationships of Enzyme Kinetics;77 10.1;3.1 Reaction Order;77 10.1.1;3.1.1 First-Order Reactions;78 10.1.2;3.1.2 Second-Order Reactions;79 10.1.3;3.1.3 Zero-Order Reactions;80 10.2;3.2 Steady-State Kinetics and the Michaelis-Menten Equation;80 10.2.1;3.2.1 Derivation of the Michaelis-Menten Equation;80 10.3;3.3 Analysis of Enzyme Kinetic Data;84 10.3.1;3.3.1 Graphic Representations of the Michaelis-Menten Equation;84 10.3.1.1;3.3.1.1 Direct and Semilogarithmic Representations;84 10.3.1.2;3.3.1.2 Direct Linear Plots;90 10.3.1.3;3.3.1.3 Linearization Methods;92 10.3.2;3.3.2 Analysis of Progress Curves;94 10.3.2.1;3.3.2.1 Integrated Michaelis-Menten Equation;95 10.3.2.2;3.3.2.2 Determination of Reaction Rates;97 10.3.2.3;3.3.2.3 Graphic Methods for Rate Determination;99 10.3.2.4;3.3.2.4 Graphic Determination of True Initial Rates;101 10.4;3.4 Reversible Enzyme Reactions;102 10.4.1;3.4.1 Rate Equation for Reversible Enzyme Reactions;102 10.4.2;3.4.2 Product Inhibition;104 10.4.3;3.4.3 The Haldane Relationship;106 10.5;References;107 11;Chapter 4 Enzyme Inhibition and Related Mechanisms;109 11.1;4.1 Unspecific and Irreversible Inhibition;109 11.1.1;4.1.1 Unspecific Inhibition;109 11.1.2;4.1.2 Irreversible Inhibition;110 11.1.2.1;4.1.2.1 General Features of Irreversible Inhibition;110 11.1.2.2;4.1.2.2 Suicide Substrates;112 11.1.2.3;4.1.2.3 Transition-State Analogs;113 11.1.2.4;4.1.2.4 Analysis of Irreversible Inhibition;114 11.2;4.2 Reversible Inhibition;116 11.2.1;4.2.1 General Rate Equation;116 11.2.1.1;4.2.1.1 Noncompetitive Inhibition and Graphic Representation of Inhibition Data;119 11.2.1.2;4.2.1.2 Competitive Inhibition;124 11.2.1.3;4.2.1.3 Uncompetitive Inhibition;128 11.2.2;4.2.2 Partial Inhibitions;130 11.2.2.1;4.2.2.1 Partially Noncompetitive Inhibition;130 11.2.2.2;4.2.2.2 Partially Uncompetitive Inhibition;132 11.2.2.3;4.2.2.3 Partially Competitive Inhibition;133 11.2.3;4.2.3 Noncompetitive and Uncompetitive Product Inhibition;135 11.2.4;4.2.4 Substrate Inhibition;136 11.3;4.3 Enzyme Reactions with Two Competing Substrates;138 11.4;4.4 Different Enzymes Catalyzing the Same Reaction;140 11.5;References;141 12;Chapter 5 Multi-Substrate Reactions;143 12.1;5.1 Nomenclature;143 12.2;5.2 Multi-Substrate Mechani