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Table Of Contents

1.1 Diffusion
1.2.1 Binding Constants
1.2.2 Derivation of the Binding Equation
1.3.1 General Binding Equation Direct Analysis Analysis of Binding Curves from Spectroscopic Titration Procedures
1.3.3 Binding of Various Ligands, Competition
1.4 Macromolecules with Non-Identical, Independent Binding Sites
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 Model
1.5.6 The Sequential Model and Negative Cooperativity
1.5.7 Physiological Aspects of Cooperativity
1.5.8 Analysis of Cooperativity Haemoglobin Aspartate Transcarbamoylase Aspartokinase Other Examples
1.6 Non-Identical, Interacting Binding Sites
1.7 References
2.1.3 Zero Order Reactions
2.2 Steady-State Kinetics and the Michaelis-Menten Equation Non-Linear Representations Direct Linear Plots Linearisation Methods Graphic Methods
2.4.1 Rate Equation for Reversible Enzyme Reactions
2.4.2 The Haldane Equation
2.4.3 Product Inhibition General Rate Equation Non-Competitive Inhibition, Graphic Representation of Inhibition Data Competitive Inhibition Uncompetitive Inhibition Partial Inhibition Mechanisms, Partially Non-Competitive Inhibition Partially Uncompetitive Inhibition Partially Competitive Inhibition Non- and Uncompetitive Product Inhibition Substrate Inhibition Distinction between Reversible and Irreversible Inhibitors Characterisation of Irreversible Inhibitions
2.5.3 Enzyme Reactions with Two Competing Substrates
2.6.1 Nomenclature
2.6.2 Random Mechanism
2.6.3 Ordered Mechanism
2.6.4 Ping-Pong Mechanism
2.6.5 Haldane Relationships in Multi-Substrate Reactions
2.6.6 Mechanisms with More than Two Substrates
2.6.7 Other Notations for Multi-Substrate Reactions
2.7.1 King-Altman Method
2.7.2 Simplified Derivations According to the Graph Theory
2.7.3 Combination of Equilibrium and Steady-State Assumptions
2.8.1 Hysteretic Enzymes
2.8.2 Kinetic Cooperativity, the Slow Transition Model Internal Diffusion Limitation Inhibition of Immobilised Enzymes pH and Temperature Behaviour of Immobilised Enzymes
2.9.2 Polymer Substrates
2.10.1 pH Optimum Curve and Determination of pK Values
2.10.2 pH Stability of Enzymes
2.10.3 Thermal Stability of Enzymes
2.10.4 Temperature Dependence of Enzyme Reactions
2.11.1 Isotope Exchange Kinetics Primary Kinetic Isotope Effect Influence of the Kinetic Isotope Effect on Vand Km Other Isotope Effects
2.12.1 General Remarks
2.12.2 Statistical Terms Used in Enzyme Kinetics
2.13 References Equilibrium Dialysis Control Experiments and Sources of Errors
3.1.2 Continuous Equilibrium Dialysis
3.1.3 Ultrafiltration The Batch Method Elution of Broad Zones The Method of Hummel and Dreyer The Brumbaugh and Ackers Method Preparative Ultracentrifugation Centrifugation Method of Chanutin et al. (1942) Sucrose Gradient Centrifugation after Draper and Hippel
3.2.4 The pH-Stat
3.2.5 Polarography
3.3 Calorimetry The Lambert-Beer Law Spectral Properties of Enzymes and Ligands Structure of Spectrophotometers Double Beam Spectrophotometer Difference Spectroscopy The Double Wavelength Spectrophotometer Photochemical Action Spectra
3.4.2 Bioluminescence Quantum Yield Perturbations of Fluorescence Measurements Fluorophores (Fluorescent Compounds) Structure of Spectrofluorimeters Radiationless Energy Transfer Fluorescence Polarisation Pulse Fluorimetry
3.4.4 Circular Dichroism and Optical Rotation Dispersion IR Spectroscopy Raman Spectroscopy Applications
3.4.6 Electron Spin Resonance Spectroscopy The Continuous Flow Method The Stopped-Flow Method Measurement of Enzyme Reactions by Flow Methods Determination of Dead Time The Temperature Jump Method The Pressure Jump Method The Electric Field Method
3.5.3 Flash Photolysis, Pico- and Femtoseconds Spectroscopy
3.5.4 Evaluation of Rapid Kinetic Reactions (Transient Kinetics)
3.6 References
6B, 25–53
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Enzyme Kinetics Principles and Methods

Enzyme Kinetics Principles and Methods

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Published by: Dinesh Kumar Selvaraj on Feb 12, 2012
Copyright:Attribution Non-commercial


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