A COMPARISON OF MUSHROOM TYROSINASE DOPAQUINONE AND DOPACHROME ASSAYS USING DIODE-ARRAY SPECTROPHOTOMETRY - DOPACHROME FORMATION VS ASCORBATE-LINKED DOPAQUINONE REDUCTION

被引：30

作者：

BEHBAHANI, I ^{[1
]}

MILLER, SA ^{[1
]}

OKEEFFE, DH ^{[1
]}

机构：

[1] UNIV MICHIGAN,DEPT CHEM,FLINT,MI 48502

来源：

MICROCHEMICAL JOURNAL | 1993年 / 47卷 / 1-2期

关键词：

D O I：

10.1006/mchj.1993.1040

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Comparisons of two assay methods for the catecholase activity of mushroom tyrosinase (EC 1.14.18.1) are reported. Tyrosinase (or polyphenol oxidase) is a widely distributed copper-containing enzyme which possesses both monooxygenase (cresolase) and oxidase (catecholase) activities. In this report the substrate employed is L-3,4-dihydroxyphenyl-alanine and the dopachrome formation and ascorbate-linked dopaquinone reduction assay methods are compared using a photodiode array spectrophotometer. This instrument has an advantage over a conventional spectrometer for kinetic studies since it is able to carry out simultaneous multiwavelength kinetic measurements at a relatively fast rate. The use of this capability in performing the two assays is described. © 1993 Academic Press. All rights reserved.

引用

页码：251 / 260

页数：10

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