
- 220 pages
- English
- PDF
- Available on iOS & Android
Principles of Enzyme Kinetics
About this book
Principles of Enzyme Kinetics discusses the principles of enzyme kinetics at an intermediate level. It is primarily written for first-year research students in enzyme kinetics. The book is composed of 10 chapters. Chapter 1 provides the basic principles of enzyme kinetics with a brief discussion of dimensional analysis. Subsequent chapters cover topics on the essential characteristics of steady-state kinetics, temperature dependence, methods for deriving steady-state rate equations, and control of enzyme activity. Integrated rate equations, and introductions to the study of fast reactions and the statistical aspects of enzyme kinetics are provided as well. Chemists and biochemists will find the book invaluable.
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Information
Table of contents
- Front Cover
- Principles of Enzyme Kinetics
- Copyright Page
- Table of Contents
- Foreword
- Preface
- Chapter 1. Basic Principles of Chemical Kinetics
- Chapter 2. Introduction to Enzyme Kinetics
- Chapter 3. How to Derive Steady-State Rate Equations
- Chapter 4. Inhibitors and Activators
- Chapter 5. Reaction Pathways
- Chapter 6. Effects of pH and Temperature on Enzymes
- Chapter 7. Control of Enzyme Activity
- Chapter 8. Analysis of Progress Curves
- Chapter 9. Fast Reactions
- Chapter 10. Estimation of Rate Constants
- References
- Index
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