Affinity Laeling of Horse‐Liver Alcohol Dehydrogenase by 3‐Chloroacetylpyridine – Adenine Dinucleotide
- 1 October 1981
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 119 (2) , 311-316
- https://doi.org/10.1111/j.1432-1033.1981.tb05610.x
Abstract
No abstract availableThis publication has 37 references indexed in Scilit:
- Evidence that Ionization of Zinc‐Bound Water Regulates the Anion‐Binding Capacity of the Coenzyme‐Binding Site in Liver Alcohol DehydrogenaseEuropean Journal of Biochemistry, 1980
- Carboxymethylation of Horse‐Liver Alcohol Dehydrogenase in the Crystalline StateEuropean Journal of Biochemistry, 1975
- Modification of alcohol dehydrogenases with two NAD+‐analogues containing reactive substituents on the functional side of the moleculeFEBS Letters, 1975
- Modification of Alcohol Dehydrogenases with a Reactive Coenzyme Analogue. Identification of Labelled Residues in the Horse-Liver and Yeast Enzymes after Treatment with Nicotinamide-5-Bromoacetyl-4-methyl-imidazole DinucleotideEuropean 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
- The structure of horse liver alcohol dehydrogenaseFEBS Letters, 1974
- Preparation of 3‐chloroacetylpyridine adenine dinucleotide: An alkylating analogue of NAD+FEBS Letters, 1974
- Anion-Binding to Liver Alcohol Dehydrogenase, Studied by Rate of AlkylationEuropean Journal of Biochemistry, 1969
- Evaluating the zinc content of horse liver alcohol dehydrogenase preparationsBiochemistry, 1969
- Über die Einwirkung von Diazomethan auf Säurechloride der PyridinreiheBerichte der deutschen chemischen Gesellschaft (A and B Series), 1940