The half-of-the-sites reactivity of horse liver alcohol dehydrogenase in the presence of alcohol substrates
- 25 September 1974
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 88 (3), 653-670
- https://doi.org/10.1016/0022-2836(74)90415-x
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Deuterium isotope effects on initial rates of the liver alcohol dehydrogenase reaction. VBiochemistry, 1973
- Approaches to the study of enzyme mechanisms lactate dehydrogenaseFEBS Letters, 1973
- Malate dehydrogenase. X. Fluorescence microtitration studies of D-malate, hydroxymalonate, nicotinamide dinucleotide, and dihydronicotinamide-adenine dinucleotide binding by mitochondrial and supernatant porcine heart enzymesBiochemistry, 1972
- Mechanistic studies on horse liver alcohol dehydrogenase. Influence of the different premixings on the transient kinetics of aldehyde reductionsBiochemistry, 1972
- Flip-Flop Mechanisms and Half-Site EnzymesCurrent Topics in Cellular Regulation, 1972
- Rapid kinetic evidence for adduct formation between the substrate analog p-nitroso-N,N-dimethylaniline and reduced nicotinamide adenine dinucleotide during enzymic reductionBiochemistry, 1971
- Flip‐Flop Mechanisms in EnzymologyEuropean Journal of Biochemistry, 1971
- Tryptophan Fluorescence Quenching in Horse Liver Alcohol DehydrogenaseEuropean Journal of Biochemistry, 1970
- Mechanistic studies on equine liver alcohol dehydrogenase. I. Stoichiometry relation of the coenzyme binding sites to the catalytic sites active in the reduction of aromatic aldehydes in the transient stateBiochemistry, 1970
- Malic DehydrogenasePublished by Elsevier ,1968