Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. I. Equilibrium and temperature-jump studies at pH 8.5 and 40 °C

Journal of Molecular Biology

Volumn 58, Issue 1, 1971, Pages 29-50

  Kirschner, Kasper ^a   Gallego, Ernesto ^a   Schuster, Inge ^a   Goodall, David ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASES; NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; DIALYSIS; ENZYMOLOGY; KINETICS; METABOLISM; PH; PROTEIN BINDING; SACCHAROMYCES; SPECTROPHOTOMETRY; TEMPERATURE;

DIALYSIS; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; HYDROGEN-ION CONCENTRATION; KINETICS; NAD; PROTEIN BINDING; SACCHAROMYCES; SPECTROPHOTOMETRY; TEMPERATURE;

EID: 0015243268     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/0022-2836(71)90230-0     Document Type: Article

References (50)

1. Regulation of Enzyme Activity and Allosteric Interactions
2. Fast Reactions and Primary Processes in Chemical Kinetics
3. The coenzyme content of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase.
4. Proc. 5th FEBS Meeting
5. Regulation of Enzyme Activity and Allosteric Interactions
6. THE BINDING OF NICOTINAMIDE-ADENINE DINUCLEOTIDE TO YEAST D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE: TEMPERATURE-JUMP RELAXATION STUDIES ON THE MECHANISM OF AN ALLOSTERIC ENZYME
7. Relaxation studies of the proflavine-DNA complex: The kinetics of an intercalation reaction
8. Determination of equilibrium constants for a number of metal-phosphate complexes