Enzyme Kinetics

Hans Bisswanger was Professor at the Interfaculty Institute of Biochemistry at the University of Tübingen (Germany), where he has developed and taught for many years an intensive course on enzyme kinetics, enzyme technology and ligand binding. His scientific interest lies with structural and regulatory mechanisms of multi-enzyme complexes, thermophilic enzymes and the technical application of immobilized enzymes. He is the author of two well-known books on enzymology that have appeared in different languages and editions.

PART I: Ligand Binding
Diffusion
Interaction between macromolecules and ligands
Identical independent binding sites
Non-identical independent binding sites
Identical interacting binding sites, cooperativity
Non-identical interacting binding sites

PART II: Enzyme Kinetics
Reaction Order
Steady-state kinetics and the Michaelis-Menten Equation
Reversible enzyme reactions
Enzyme inhibition
Multi-substrate reactions
Rate equations of complex enzyme mechanisms
Allosteric enzymes
pH and temperature dependence
Isotope exchange kinetics and isotope effects
Ribozymes
Enyzmes with polymeric substrates
Immobilized enzymes
Kinetics of transport processes
Enzyme reactions at membrane interfaces

PART III: Methods
Methods for investigating multiple equilibria
Electrochemical methods
Calorimetry
Spectroscopic methods
Measurement of fast reactions