Abstract
The Oxidation of Tyramine, Tyrosine, and Related Compounds by Peroxidase
Highlights
RF values are given for tyramine (Ta) and tyrosine (To) spots
The tyrosyl groups in bovine fibrinogen, insulin, and pepsin were found to be unreactive with external tyrosine or tyramine in the presence of peroxidase and hydrogen peroxide, nor could one tyrosyl group form a diphenyl linkage with another tyrosyl group in the protein
A brown pigment, which separated from the reaction mixture, was shown to contain dityramine and more extensively oxidized and polymerized derivatives, and to be nonhomogeneous
Summary
RF values are given for tyramine (Ta) and tyrosine (To) spots. Solvents employed: for (I), n-butanol-formic acid (88 per cent) water, (75: 10: 15) ; for [2], n-butanol-acetic acid-water,. The ether was evaporated, and the derivative recrystallized several times from the ethanol-water mixture until white, rhombic crystals were obtained; m.p. 173” (corrected). Compound II-HCl produced a yellow color with Millon’s reagent and was ninhydrin-positive It fluoresced under ultraviolet light, its ultraviolet absorption spectrum (Fig. 4) was similar to that of Compound I. The methylated derivative is characterized by a strong absorption maximum at 283 mp and a minimum at 260 rnp Elementary analyses of this compound, consistent with a terphenyl structure for Compound II, are inconclusive because the sample was contaminated with salt. The pigment produced in the tyramine-peroxidase system seemed to be composed of monomers similar to Compounds I and II, as well as more highly oxidized substances, all of which were tightly bound into a nonhomogeneous polymer. With the exception of diiodotyrosine and methyl salicylate, all substrates with free phenolic groups
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