Identification of a reactive arginyl residue in horse liver alcohol dehydrogenase
- 1 July 1977
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 77 (1), 73-78
- https://doi.org/10.1016/s0006-291x(77)80166-6
Abstract
No abstract availableThis publication has 11 references indexed in Scilit:
- Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolutionJournal of Molecular Biology, 1976
- Amino acid sequence around a reactive cysteine of yeast alcohol dehydrogenaseBiochemical and Biophysical Research Communications, 1975
- Role of arginyl residues in directing carboxymethylation of horse liver alcohol dehydrogenaseBiochemistry, 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
- Functional arginyl residues as NADH binding sites of alcohol dehydrogenasesBiochemistry, 1974
- Functional arginyl residues in carboxypeptidase A. Modification with butanedioneBiochemistry, 1973
- Reactive lysine residues in horse liver alcohol dehydrogenaseBiochemical and Biophysical Research Communications, 1973
- [33] Specific modification of NH2-terminal residues by transaminationMethods in Enzymology, 1972
- Horse Liver Alcohol DehydrogenaseEuropean Journal of Biochemistry, 1970