1;Cover;12;Title Page;33;Copyright;64;Contents;75;Preface to the Third Edition;176;List of Abbreviations and Symbols;197;Chapter 1 General Aspects of Enzyme Analysis;217.1;1.1 Introduction and Essentials for Enzyme Assays;217.2;1.2 Theoretical Basis of Enzyme Assays;247.2.1;1.2.1 Order of Enzyme Reactions;247.2.2;1.2.2 Importance of the Reaction Order for Enzyme Reactions;267.2.3;1.2.3 The Reaction Velocity, Significance, and Practical Aspects;307.2.3.1;1.2.3.1 Determination of the Reaction Velocity, the Progress Curve;307.2.3.2;1.2.3.2 Enzyme Units;357.2.3.3;1.2.3.3 A Short Discussion About Errors in Enzyme Assays;377.2.3.4;1.2.3.4 Practical Rules for the Preparation of Dilution Series;417.2.3.5;1.2.3.5 Statistical Treatment of Enzyme Reactions;437.2.4;1.2.4 Treatment of the Michaelis-Menten Equation;447.2.4.1;1.2.4.1 General Considerations;447.2.4.2;1.2.4.2 Linear Representations of the Michaelis-Menten Equation;467.2.5;1.2.5 Enzyme Inhibition;487.2.6;1.2.6 Multisubstrate Reactions;537.3;1.3 Essential Conditions for Enzyme Assays;557.3.1;1.3.1 Dependence on Solvents and Ionic Strength;557.3.2;1.3.2 pH Dependency;567.3.2.1;1.3.2.1 Isoelectric Point;587.3.2.2;1.3.2.2 Buffers: What Must Be Regarded?;587.3.2.3;1.3.2.3 How to Prepare Buffers?;617.3.3;1.3.3 Temperature Dependency;627.3.4;1.3.4 Stability of Enzymes;677.3.4.1;1.3.4.1 Why Are Enzymes Unstable?;677.3.4.2;1.3.4.2 How Can Enzymes Be Stabilized?;687.3.4.3;1.3.4.3 How to Store Enzymes?;687.4;1.4 Theory of Coupled Enzyme Reactions;717.4.1;1.4.1 Two Coupled Reactions;717.4.2;1.4.2 Three Coupled Reactions;747.5;1.5 Substrate Determination;747.5.1;1.5.1 End Point Method;757.5.2;1.5.2 Substrate Determination by Coupled Enzyme Reactions;767.5.3;1.5.3 Kinetic Method for Substrate Determination;777.5.4;1.5.4 Enzymatic Cycling;778;Chapter 2 Instrumental Aspects;818.1;2.1 Spectroscopic Methods;818.1.1;2.1.1 Absorption (UV/Vis) Photometry;818.1.2;2.1.2 Cuvettes;928.1.2.1;2.1.2.1 Shape;928.1.2.2;2.1.2.2 Material;938.1.2.3;2.1.2.3 Cleaning;938.1.3;2.1.3 Turbidity Measurement;948.1.4;2.1.4 Fluorescence Photometry;958.1.5;2.1.5 Luminometry;998.1.6;2.1.6 Polarimetry;1008.2;2.2 Electrochemical Methods;1018.2.1;2.2.1 pH Meter and Glass Electrodes;1018.2.2;2.2.2 pH Stat;1028.2.3;2.2.3 Potentiometry;1038.2.4;2.2.4 Oxygen and Carbon Dioxide Electrodes;1038.3;2.3 Radioactive Labeling;1048.4;2.4 Diverse Methods;1049;Chapter 3 Enzyme Assays;1079.1;3.1 Enzyme Nomenclature;1089.2;3.2 Practical Considerations for Enzyme Assays;11010;Chapter 4 Oxidoreductases, EC 1;11510.1;4.1 General Assay Procedures;11510.1.1;4.1.1 Optical Assay;11510.1.2;4.1.2 Fluorimetric Assay;11610.2;4.2 Alcohol Dehydrogenase (ADH), EC 1.1.1.1;11610.2.1;4.2.1 Reduction Assay;11610.2.2;4.2.2 Oxidation Assay;11710.3;4.3 Alcohol Dehydrogenase (NADP+), EC 1.1.1.2;11810.4;4.4 Homoserine Dehydrogenase, EC 1.1.1.3;11910.5;4.5 Shikimate Dehydrogenase, EC 1.1.1.25;12010.6;4.6 l?Lactate Dehydrogenase (LDH), EC 1.1.1.27;12110.6.1;4.6.1 Photometric Reduction Assay;12110.6.2;4.6.2 Fluorimetric Reduction Assay;12210.6.3;4.6.3 Oxidation Assay;12310.7;4.7 Malate Dehydrogenase (MDH), EC 1.1.1.37;12410.8;4.8 Malate Dehydrogenase (Oxaloacetate?Decarboxylating) (NAD+), EC 1.1.1.38, and Malate Dehydrogenase (Decarboxylating), EC 1.1.1.39;12510.9;4.9 Malate Dehydrogenase (Oxaloacetate?decarboxylating) (NADP+), EC 1.1.1.40;12610.10;4.10 Isocitrate Dehydrogenase (NAD+) (ICDH), EC 1.1.1.41;12710.11;4.11 Isocitrate Dehydrogenase (NADP+) (ICDH), EC 1.1.1.42;12810.12;4.12 Glucose?6?Phosphate Dehydrogenase (NADP+), EC 1.1.1.49 (G6PDH);12910.13;4.13 Glucose Oxidase (GOD), EC 1.1.3.4;13010.14;4.14 Formate Dehydrogenase (FDH), EC 1.2.1.2;13110.15;4.15 Glyceraldehyde?3?Phosphate Dehydrogenase (GAPDH), EC 1.2.1.12;13210.15.1;4.15.1 Oxidation Assay;13210.15.2;4.15.2 Reduction Assay Coupled with 3?Phosphoglycerate Kinase (PGK);13310.16;4.16 Long?Chain?Aldehyde Dehydrogenase, E