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, 222 (2), 407-11

Oxidation of Tyrosine Residues in Proteins by Tyrosinase. Formation of Protein-Bonded 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4-dihydroxyphenylalanine

Oxidation of Tyrosine Residues in Proteins by Tyrosinase. Formation of Protein-Bonded 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4-dihydroxyphenylalanine

S Ito et al. Biochem J.

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.

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References

    1. Biochemistry. 1967 Jan;6(1):116-20 - PubMed
    1. J Biol Chem. 1959 Dec;234:3291-5 - PubMed
    1. J Med Chem. 1976 Jan;19(1):37-40 - PubMed
    1. J Invest Dermatol. 1976 Jul;67(1):72-89 - PubMed
    1. Nature. 1966 Feb 26;209(5026):888-90 - PubMed

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