Frontmatter -- Opening Remarks And Deface -- Contents -- List Of Contributors -- Section I. Primary Structure And Conformation -- Conformational Adaptations Among Dehydrogenases -- The Primary Structures Of Chicken Lactate Dehydrogenase M4 And H4 Isoenzymes -- Structure And Properties Of Glyceraldehyde 3-Phosphate Dehydrogenase From Thermophilic Microorganisms -- Comparative Aspects Of Structural Studies Of Alcohol Dehydrogenases -- X-ray Diffraction Studies on Sheep Liver 6-Phosphogluconate Dehydrogenase at 6Å Resolution -- Section II. Symmetry and Coenzyme Binding -- Conformational Changes and Non-Equivalence in the Binding of NAD+ to Cytoplasmic Malate Dehydrogenase -- The Effect of Nucleotide Binding on Subunit Interactions in Glyceraldehyde 3-Phosphate Dehydrogenase as Determined by the Kinetics and Thermodynamics of Subunit Exchange -- Dinucleotide Dependent Conformational and Chemical Bonding Changes in Muscle Glyceraldehyde-3-PO4 Dehydrogenase -- Non Equivalent Active Sites in Transient Kinetics of Sturgeon Glyceraldehyde-3-Phosphate Dehydrogenase -- Symmetry and NAD+ -Dependent Structural Changes in D-Glyceraldehyde- 3-Phosphate Dehydrogenase -- The Unimer Model of Glutamate Dehydrogenase: A Verification Using Chemical Modification -- The Immobilization Technique as an Aid in the Study of the Quaternary Structure of Dehydrogenases with Special Reference to Subunit Association and Allosteric Regulation -- Section III. Chemical Mechanism and Coenzyme Binding -- On the mode of hydrogen transfer and catalysis in nicotinamide-dependent oxidoreduction -- Spectrophotometric and Kinetic Identification of Transient Intermediates in the Horse Liver Alcohol Dehydrogenase Catalyzed Reduction of some Aromatic Substrates -- Conformation of NAD+ in Solution, in Holoenzymes and in the Crystalline Li+ Complex -- Conformation of ɛNAD+ in Solution and Bound to Dehydrogenases Revealed by Fluorescence Decay Kinetics -- Affinity labeling by alkylating analogues of NAD -- Immobilized Adenine Coenzymes in General Ligand Affinity Chromatography and their Use as Active Coenzymes -- The Interaction of Glutamate Dehydrogenase with Ligands -- Thermodynamics of the LDH Reaction -- The Equilibrium NADH + NADP+=NAD+ + NADPH as Studied by Transhydrogenase -- Section IV. Structure Function Relationship -- Functional Significance of the Structure of Liver Alcohol Dehydrogenase -- Substrate Orientation in the Active Site of Liver Alcohol Dehydrogenase -- Equilibrium Studies and Kinetics of Reactivation, Refolding and Reassociation of Lactic Dehydrogenase and Glyceraldehyde-3- Phosphate Dehydrogenase -- Studies on Dehydrogenases from Halobacterium of the Dead Sea -- Organization of a Bifunctional Enzyme: Escherichia Coli Aspartokinase I-Homoserine Dehydrogenase I. Relationships between the Catalytic and Regulatory Functions -- Chemical Probes of Topography and Subunit Interactions in a Simple Dehydrogenase and a Multienzyme Complex -- Section V. Kinetics and Regulation -- Pressure Relaxation of the Equilibrium of the Reaction Catalyzed by Pig Heart Lactate Dehydrogenase: a Test of the Kinetic Mechanism -- The Role of Conformational Changes in the Liver Alcohol Dehydrogenase Reaction Mechanism -- The Mechanism of Glutamate Dehydrogenase: Some Kinetic Aspects -- Regulation of Isociträte Oxidation by TPN- and DPN-Isociträte Dehydrogenases -- Cinnamoyl-CoA:NADPH Oxidoreductase and Cinnamyl Alcohol Dehydrogenase: two Enzymes of Lignin Monomer Biosynthesis -- Octopine Dehydrogenase. Spectroscopic and Conformational Properties of Bound Coenzyme, and a Possible Temperature-Regulation Function -- An Oil-Water-Histidine Mechanism for the Activation of Coenzyme in the a-Hydroxyacid Dehydrogenases -- Concluding Remarks -- Index of Contributors -- Subject Index -- Backmatter

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