Functional arginine residues involved in coenzyme binding by glutamate dehydrogenases
Open Access
- 1 August 1975
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 250 (16) , 6555-6559
- https://doi.org/10.1016/s0021-9258(19)41101-0
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase of Neurospora. III. Inactivation by nitration of a tyrosine residue involved in coenzyme bindingJournal of Biological Chemistry, 1975
- Nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase of Neurospora.Journal of Biological Chemistry, 1975
- Reversible modification of arginine residues. Application to sequence studies by restriction of tryptic hydrolysis to lysine residuesJournal of Biological Chemistry, 1975
- Amino-Acid Sequence of NADP-Specific Glutamate Dehydrogenase of Neurospora crassaProceedings of the National Academy of Sciences, 1974
- Functional arginyl residues as NADH binding sites of alcohol dehydrogenasesBiochemistry, 1974
- Selective chemical modification of arginine residues in mitochondrial malate dehydrogenaseBiochemical and Biophysical Research Communications, 1974
- Mechanism of inactivation of L-glutamate dehydrogenase by pyridoxal and pyridoxal phosphateBiochemistry, 1973
- Functional arginyl residues in carboxypeptidase A. Modification with butanedioneBiochemistry, 1973
- Structure-Function Relationships in Lactate DehydrogenaseProceedings of the National Academy of Sciences, 1973
- Automatic Recording Apparatus for Use in Chromatography of Amino AcidsAnalytical Chemistry, 1958