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

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

Published:1983-01 Issue:1 Volume:258 Page:497-502
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Swenson R P,Williams C H,Massey V

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference23 articles.

1. Chemical modifications of D-amino acid oxidase. Evidence for active site histidine, tyrosine, and arginine residues.

2. Studies on the Elimination Reaction of d-Amino Acid Oxidase with α-Amino-β-chlorobutyrate

3. Effect of pH on the interaction of benzoate and D-amino acid oxidase

4. Chemical modification of D-amino acid oxidase. Amino acid sequence of the tryptic peptides containing tyrosine and lysine residues modified by fluorodinitrobenzene.

5. The primary structure of D-amino acid oxidase from pig kidney. I. Isolation and sequence of the tryptic peptides.

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