Oxidation of tyrosine residues in proteins by tyrosinase. Formation of protein-bonded 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4-dihydroxyphenylalanine.
Biochem J
; 222(2): 407-11, 1984 Sep 01.
Article
en En
| MEDLINE
| ID: mdl-6433900
ABSTRACT
A simple and rapid method was developed for the determination of 3,4-dihydroxyphenylalanine (dopa) and 5-S-cysteinyl-3,4-dihydroxyphenylalanine (5-S-cysteinyldopa) in proteins with the use of high-pressure liquid chromatography. With this method, it is demonstrated that mushroom tyrosinase can catalyse hydroxylation of tyrosine residues in proteins to dopa and subsequent oxidation to dopaquinone residues. The dopaquinone residues in proteins combine with cysteine residues to form 5-S-cysteinyldopa in bovine serum albumin and yeast alcohol dehydrogenase, whereas dopa is the major product in bovine insulin, which lacks cysteine residues.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Tirosina
/
Proteínas
/
Dihidroxifenilalanina
/
Catecol Oxidasa
/
Monofenol Monooxigenasa
Idioma:
En
Revista:
Biochem J
Año:
1984
Tipo del documento:
Article