Properties of horse liver alcohol dehydrogenase modified by the affinity label 3-chloroacetylpyridine-adenine dinucleotide
- 31 October 1983
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 748 (3) , 362-366
- https://doi.org/10.1016/0167-4838(83)90180-2
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Affinity Laeling of Horse‐Liver Alcohol Dehydrogenase by 3‐Chloroacetylpyridine – Adenine DinucleotideEuropean Journal of Biochemistry, 1981
- Phosphate Binding to Liver Alcohol Dehydrogenase Studied by the Rate of Alkylation with Affinity LabelsEuropean Journal of Biochemistry, 1980
- Ambivalent active-site-directed inactivators of liver alcohol dehydrogenaseBiochemistry, 1978
- Effect of Substrate Structure on the Pre‐Steady‐State Kinetics of Oxidation by Liver Alcohol DehydrogenaseEuropean Journal of Biochemistry, 1975
- The half-of-the-sites reactivity of horse liver alcohol dehydrogenase in the presence of alcohol substratesJournal of Molecular Biology, 1974
- Preparation of 3‐chloroacetylpyridine adenine dinucleotide: An alkylating analogue of NAD+FEBS Letters, 1974
- Heterogeneity of Horse Liver Alcohol DehydrogenaseEuropean Journal of Biochemistry, 1970
- Structure and Function Relationships in Isoenzymes of Horse Liver Alcohol DehydrogenaseNature, 1969
- Facilitated Proton Transfer in Enzyme CatalysisScience, 1968
- Proposed Catalytic Role for Histidine in Pyridine Nucleotide-linked Alcohol DehydrogenasesNature, 1966