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Your search keyword '"Cross, D."' showing total 13 results
Start Over Author "Cross, D." Topic glutamate dehydrogenase
13 results on '"Cross, D."'

1. Two-step binding of adenosine diphosphate to L-glutamate dehydrogenase. Effect on the binding of reduced nicotinamide adenine diphosphate and on enzymatic catalysis.

Author

Colen AH, Cross DG, and Fisher HF

Subjects
Adenosine Diphosphate pharmacology, Animals, Catalysis, Cattle, Chromatography, Gel, Computers, Isomerism, Kinetics, Ligands, Liver enzymology, Mathematics, Models, Chemical, Oxidation-Reduction, Protein Binding, Spectrophotometry, Ultraviolet, Temperature, Adenosine Diphosphate metabolism, Glutamate Dehydrogenase metabolism, NADP metabolism
Published
1974
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2. Hydrogen exchange at the amide group of reduced pyridine nucleotides and the inhibition of that reaction by dehydrogenases.

Author

Cross DG, Brown A, and Fisher HF

Subjects
Animals, Cattle, Hydrogen-Ion Concentration, Liver enzymology, Oxidation-Reduction, Protein Binding, Saccharomyces cerevisiae enzymology, Spectrophotometry, Ultraviolet, Alcohol Oxidoreductases metabolism, Glutamate Dehydrogenase metabolism, L-Lactate Dehydrogenase metabolism, NAD, NADP, Nicotinamide Mononucleotide, Ribonucleotides
Abstract

Stopped flow ultraviolet spectroscopy has been used to measure the rate of hydrogen exchange with solvent at the amide group of reduced nicotinamide nucleotide coenzymes. Several mechanisms for the exchange reaction are considered in the light of the kinetic data. Complex formation between the coenzyme and any of four dehydrogenases markedly slows the rate of hydrogen exchange. Hydrogen bond formation and/or hydrophobic interactions within these complexes are thought to be the reasons for the decreased rate of exchange.

Published
1976

7. The binding of -ketoglutarate in a binary complex and in a ternary complex with NADP + by L-glutamate dehydrogenase.

Author

Cross DG, McGregor LL, and Fisher HF

Subjects
Animals, Binding Sites, Catalysis, Cattle, Chemical Phenomena, Chemistry, Glutamates, Kinetics, Liver enzymology, Mathematics, Molecular Weight, Niacinamide, Oxidation-Reduction, Protein Binding, Spectrophotometry, Ultraviolet, Structure-Activity Relationship, Tryptophan, Glutamate Dehydrogenase, Ketoglutaric Acids, NADP
Published
1972
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9. Dehydrogenae-reduced coenzyme difference spectra, their resolution and relationship to the stereospecificity of hydrogen transfer.

Author

Fisher HF, Adija DL, and Cross DG

Subjects
Animals, Binding Sites, Cattle, Glyceraldehyde-3-Phosphate Dehydrogenases, Glycerolphosphate Dehydrogenase, Horses, Hydroxysteroid Dehydrogenases, Isocitrate Dehydrogenase, L-Lactate Dehydrogenase, Liver enzymology, Malate Dehydrogenase, Methods, Muscles enzymology, Rabbits, Saccharomyces enzymology, Spectrophotometry, Streptomyces enzymology, Swine, Ultraviolet Rays, Alcohol Oxidoreductases, Glutamate Dehydrogenase, Hydrogen, NAD, NADP
Published
1969
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10. Enzyme-coenzyme complexes of pyridine nucleotide-linked dehydrogenases.

Author

Fisher HF and Cross DG

Subjects
Spectrophotometry, Alcohol Oxidoreductases, Glutamate Dehydrogenase, Isocitrate Dehydrogenase, NAD, NADP
Abstract

Enzyme-reduced coenzyme binary complexes produce previously unreported shifts in the spectrum of the free coenzyme. These shifts give rise to difference spectra which resemble a general environmental change for reduced diphosphopyridine nucleotide (DPNH) in the glutamic dehydrogenase-DPNH complex, and indicate a more specific enzyme-coenzyme interaction for yeast alcohol dehydrogenase-DPNH, isocitrate dehydrogenase-TPNH, and lactic dehydrogenase-DPNH complexes.

Published
1966
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