دانلود کتاب Pyridine Nucleotide-Dependent Dehydrogenases: Proceedings of the second International Symposium held at the University of Konstanz, West Germany. March 28–April 1, 1977

فهرست مطالب :

Opening Remarks And Deface\nContents\nList Of Contributors\nSection I. Primary Structure And Conformation\nConformational Adaptations Among Dehydrogenases\nThe Primary Structures Of Chicken Lactate Dehydrogenase M₄ And H₄ Isoenzymes\nStructure And Properties Of Glyceraldehyde 3-Phosphate Dehydrogenase From Thermophilic Microorganisms\nComparative Aspects Of Structural Studies Of Alcohol Dehydrogenases\nX-ray Diffraction Studies on Sheep Liver 6-Phosphogluconate Dehydrogenase at 6Å Resolution\nSection II. Symmetry and Coenzyme Binding\nConformational Changes and Non-Equivalence in the Binding of NAD⁺ to Cytoplasmic Malate Dehydrogenase\nThe Effect of Nucleotide Binding on Subunit Interactions in Glyceraldehyde 3-Phosphate Dehydrogenase as Determined by the Kinetics and Thermodynamics of Subunit Exchange\nDinucleotide Dependent Conformational and Chemical Bonding Changes in Muscle Glyceraldehyde-3-PO₄ Dehydrogenase\nNon Equivalent Active Sites in Transient Kinetics of Sturgeon Glyceraldehyde-3-Phosphate Dehydrogenase\nSymmetry and NAD⁺ -Dependent Structural Changes in D-Glyceraldehyde- 3-Phosphate Dehydrogenase\nThe Unimer Model of Glutamate Dehydrogenase: A Verification Using Chemical Modification\nThe Immobilization Technique as an Aid in the Study of the Quaternary Structure of Dehydrogenases with Special Reference to Subunit Association and Allosteric Regulation\nSection III. Chemical Mechanism and Coenzyme Binding\nOn the mode of hydrogen transfer and catalysis in nicotinamide-dependent oxidoreduction\nSpectrophotometric and Kinetic Identification of Transient Intermediates in the Horse Liver Alcohol Dehydrogenase Catalyzed Reduction of some Aromatic Substrates\nConformation of NAD⁺ in Solution, in Holoenzymes and in the Crystalline Li⁺ Complex\nConformation of ɛNAD⁺ in Solution and Bound to Dehydrogenases Revealed by Fluorescence Decay Kinetics\nAffinity labeling by alkylating analogues of NAD\nImmobilized Adenine Coenzymes in General Ligand Affinity Chromatography and their Use as Active Coenzymes\nThe Interaction of Glutamate Dehydrogenase with Ligands\nThermodynamics of the LDH Reaction\nThe Equilibrium NADH + NADP⁺\\=\\NAD⁺ + NADPH as Studied by Transhydrogenase\nSection IV. Structure Function Relationship\nFunctional Significance of the Structure of Liver Alcohol Dehydrogenase\nSubstrate Orientation in the Active Site of Liver Alcohol Dehydrogenase\nEquilibrium Studies and Kinetics of Reactivation, Refolding and Reassociation of Lactic Dehydrogenase and Glyceraldehyde-3- Phosphate Dehydrogenase\nStudies on Dehydrogenases from Halobacterium of the Dead Sea\nOrganization of a Bifunctional Enzyme: Escherichia Coli Aspartokinase I-Homoserine Dehydrogenase I. Relationships between the Catalytic and Regulatory Functions\nChemical Probes of Topography and Subunit Interactions in a Simple Dehydrogenase and a Multienzyme Complex\nSection V. Kinetics and Regulation\nPressure Relaxation of the Equilibrium of the Reaction Catalyzed by Pig Heart Lactate Dehydrogenase: a Test of the Kinetic Mechanism\nThe Role of Conformational Changes in the Liver Alcohol Dehydrogenase Reaction Mechanism\nThe Mechanism of Glutamate Dehydrogenase: Some Kinetic Aspects\nRegulation of Isociträte Oxidation by TPN- and DPN-Isociträte Dehydrogenases\nCinnamoyl-CoA:NADPH Oxidoreductase and Cinnamyl Alcohol Dehydrogenase: two Enzymes of Lignin Monomer Biosynthesis\nOctopine Dehydrogenase. Spectroscopic and Conformational Properties of Bound Coenzyme, and a Possible Temperature-Regulation Function\nAn Oil-Water-Histidine Mechanism for the Activation of Coenzyme in the a-Hydroxyacid Dehydrogenases\nConcluding Remarks\nIndex of Contributors\nSubject Index