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" Pyridine Nucleotide-Dependent Dehydrogenases : "
edited by Horst Sund.
Document Type
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BL
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Record Number
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714312
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Doc. No
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b536462
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Main Entry
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edited by Horst Sund.
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Title & Author
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Pyridine Nucleotide-Dependent Dehydrogenases : : Proceedings of an Advanced Study Institute held at the University of Konstanz, Germany, September 15-20, 1969\ edited by Horst Sund.
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Publication Statement
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Berlin, Heidelberg: Springer Berlin Heidelberg, 1970
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Page. NO
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(xv, 472 pages)
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ISBN
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3642499740
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: 9783642499746
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Contents
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Opening Remarks --;Section I General --;Kinetics --;The Mechanism of Hydride Transfer --;The Significance of the Investigation of Model Compounds for the Elucidation of the Mechanism of Hydrogen-Transfer with Pyridine Nucleotides --;The Structure of Pyridine Coenzymes as Related to Binding --;Section II Structure and Function of Dehydrogenases --;The Primary Structure and Activity of Glyceraldehyde 3-Phosphate Dehydrogenase --;Quaternary Structure and Conformation of Lactic Dehydrogenase and Glyceraldehyde-3-Phosphate Dehydrogenase --;The Stereoselective Inhibition of Functional --;SH Groups of Dehydrogenases --;The Role of Zinc Ions, --;SH Groups, and Histidyl Residues in the Mechanism of Dehydrogenases --;Section III Alcohol and Lactate Dehydrogenases --;Structural and Functional Relationships between Isoenzymes of Horse LADH --;X-Ray Studies of Horse Liver Alcohol Dehydrogenase --;Lactate Dehydrogenase --;Studies on Structure and Active Sites of Lactate Dehydrogenase from Pig Heart and Pig Muscle --;Structure and Mechanism of Lactate Dehydrogenase --;Section IV Glyceraldehyde-3-Phosphate Dehydrogenases --;Selective Reactivity of Functional Groups in Glyceraldehyde 3-Phosphate Dehydrogenase --;On the Relationship between Protein Conformation and Enzyme-Substrate Covalent Bond Formation in Glyceraldehyde-3-Phosphate Dehydrogenase --;Cooperative Phenomena in Yeast Glyceraldehyde-3-Phosphate Dehydrogenase --;Conformational Effects of NAD+ on Yeast Glyceraldehyde-3-Phosphate Dehydrogenase --;Recent Studies on the Allosteric Glyceraldehyde-3-Phosphate Dehydrogenase from Yeast --;Subunit Interactions in Glyceraldehyde-3-Phosphate Dehydrogenase: A Fluorometric and Calorimetric Analysis of DPN Binding as a Function of Temperature --;Muscle Glyceraldehydephosphate Dehydrogenase: NAD+ Binding and its Implications for the Mechanism of Action of the Enzyme --;Section V Glutamate Dehydrogenases --;Kinetics and Mechanism of Glutamate Dehydrogenase --;Optical Probes for Glutamate Dehydrogenase --;Glutamate Dehydrogenase --;A Study on its Inactivation --;Quaternary Structure and Enzymic Properties of Beef Liver Glutamate Dehydrogenase --;Structure and Association of Glutamate Dehydrogenase Solutions --;Mechanism of Action of Glutamate Dehydrogenase from Various Sources --;Section VI Different Aspects of Reactions Catalyzed by Dehydrogenases --;Kinetic Studies of NADP-Dependent Isocitrate Dehydrogenase from Beef Heart Mitochondria --;The Role of NAD-Linked Dehydrogenases in the Biosynthesis of UDP-D-Xylose --;Regulation by NADP+ and NADPH of Transhydrogenase from Azotobacter Vinelandii --;Activation Effect of 2?-Adenylic Acid on Bacterial Transhydrogenases --;Section VII Pyridine Nucleotide-Dependent Flavin Enzymes --;The Role of NAD+ in the Catalytic Mechanism of Lipoamide Dehydrogenase --;The NADH Dehydrogenase of the Respiratory Chain --;A New Intermediate in TPNH-Linked Flavoproteins --;Section VIII Metabolic Aspects --;Regulation of the Redox State of the Pyridine Nucleotides in Rat Liver --;The State of the DPN System in Liver. An Analysis of Pyridine Nucleotide Levels, Surface Fluorescence, and Redox Potentials of Indicator Metabolite Couples in the Hemoglobin-Free Perfused Rat Liver --;Closing Remarks --;Index of Contributors.
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Abstract
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The present volume represents the proceedings of the symposium on npyridine Nucleotide-Dependent Dehydrogenases" which was held on the campus of the re- cently established University of Konstanz, Germany, from September 15 to 20, 1969.
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Subject
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Medicine.
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Added Entry
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Horst Sund
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