Essential arginine residues in beef kidney D-aspartate oxidase (a preliminary report)
- 1 August 1977
- journal article
- research article
- Published by Springer Nature in Molecular and Cellular Biochemistry
- Vol. 17 (1), 7-9
- https://doi.org/10.1007/bf01732548
Abstract
Summary Partially purifiedD-aspartate oxidase from beef kidney has been tested in the presence of butanedione or phenylglyoxal, which specifically modify the arginine molecule. The results obtained clearly indicate that arginine residues are involved in the binding of the substrate to the active site of the enzyme.Keywords
This publication has 8 references indexed in Scilit:
- Essential arginine residues in glutamate dehydrogenaseFEBS Letters, 1976
- A spectrophotometric procedure for determining the activity of various rat tissue oxidasesAnalytical Biochemistry, 1975
- Essential arginyl residues in aspartate aminotransferasesBiochemical and Biophysical Research Communications, 1975
- Functional arginyl residues as NADH binding sites of alcohol dehydrogenasesBiochemistry, 1974
- Functional arginyl residues in carboxypeptidase A. Modification with butanedioneBiochemistry, 1973
- Partial purification and some properties of beef kidney D-aspartate oxidase.1971
- The Reaction of Phenylglyoxal with Arginine Residues in ProteinsJournal of Biological Chemistry, 1968