Subunit interactions in liver alcohol dehydrogenase
- 1 September 1977
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 115 (3) , 355-380
- https://doi.org/10.1016/0022-2836(77)90159-0
Abstract
No abstract availableThis publication has 21 references indexed in Scilit:
- Carboxymethylated Liver Alcohol DehydrogenaseEuropean Journal of Biochemistry, 1976
- The Role of Negative Cooperativity and Half-of-the-Sites Reactivity in Enzyme RegulationCurrent Topics in Cellular Regulation, 1976
- Functional arginyl residues as NADH binding sites of alcohol dehydrogenasesBiochemistry, 1974
- The half-of-the-sites reactivity of horse liver alcohol dehydrogenase in the presence of alcohol substratesJournal of Molecular Biology, 1974
- Roles of zinc ion and reduced coenzyme in the formation of a transient chemical intermediate during the equine liver alcohol dehydrogenase catalyzed reduction of an aromatic aldehydeBiochemistry, 1973
- Mechanistic studies on horse liver alcohol dehydrogenase. Influence of the different premixings on the transient kinetics of aldehyde reductionsBiochemistry, 1972
- Role of zinc in horse liver alcohol dehydrogenase. II. Coenzyme and substrate bindingBiochemistry, 1972
- Heterogeneity of 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
- Reactivity and Function of Sulfhydryl Groups in Horse Liver Alcohol Dehydrogenase*Biochemistry, 1965