Enzyme Kinetics

Principles and Methods
2. überarbeitete und aktualisierte Auflage 2008
ISBN: 978-3-527-31957-2
Verlag: Wiley-VCH

Buch, Englisch, 302 Seiten, Format (B × H): 170 mm x 240 mm, Gewicht: 768 g

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.

Autoren/Hrsg.

Bisswanger, Hans

Inhaltsverzeichnis

Symbols and Abbreviations
Introduction
Multiple Equilibria
- Diffusion
- Interaction of ligands with macromolecules
o Macromolecules with identical, non-identical, independent and interacting binding sites
Enzyme Kinetics
- reaction order
- kinetics,
o analysis of kinetic data, enzyme inhibition, multi-substrate reactions,
o analysis of complex enzyme mechanisms, allosteric enzymes,
- PH, temperature dependence of enzymes
- Isotope exchange
- Statistical methods in enzyme kinetics
Methods
- methods for the investigation of multiple equilibria, electrochemical methods, spetroscopy, calorimetry, measurements of fast reactions
Index

Über Autor(innen)

Prof. Dr. Hans Bisswanger is currently at the Interfaculty Institute of Biochemistry at the University of Tübingen. He has developed and leads an intensive course on enzyme kinetics, enzyme technology and ligand binding, while his main focus is on structural and regulatory mechanisms of multi-enzyme complexes and temperature stable enzyme complexes. He is also working on the gentle immobilization of enzyme activities on synthetic surfaces, a method which has been favorably applied for the restoration of damaged documents.