Work

Identification of the histidine residue in D-amino acid oxidase that is covalently modified during inactivation by 5-dimethylaminonaphthalene-1-sulfonyl chloride.

Year: 1983

Type: article

Abstract: The flavoprotein D-amino acid oxidase is inactivated during covalent modification of predominantly a histidine residue(s) by a low molar excess of 5-dimethylaminonaphthalene-1-sulfonyl (dansyl) chloride a t pH 6.6 (Nishino, T., Massey, V., and Williams, C. H., Jr. (1980)

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)33283-6

Authors: R P Swenson, C H Williams, V Massey

Institutions: University of Michigan, Ann Arbor VA Medical Center

Language: English

Topic: Amino Acid Enzymes and Metabolism

Subfield: Biochemistry

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1606865708

FWCI: 1.678

Cites: 20

Cited by: 19

Related to: 10