THE LOW-ISOELECTRIC POINT TYROSINASE OF AGARICUS-BISPORUS MAY BE A GLYCOPROTEIN

被引：32

作者：

GERRITSEN, YAM ^{[1
]}

CHAPELON, CGJ ^{[1
]}

WICHERS, HJ ^{[1
]}

机构：

[1] AGROTECHNOL RES INST,6700 PM WAGENINGEN,NETHERLANDS

来源：

PHYTOCHEMISTRY | 1994年 / 35卷 / 03期

关键词：

AGARICUS BISPORUS; BASIDIOMYCOTINA; FUNGUS; MUSHROOM; POLYPHENOL OXIDASE; TYROSINASE; GLYCOPROTEIN;

D O I：

10.1016/S0031-9422(00)90563-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Tyrosinase (EC1.14.18.1) of Agaricus bisporus occurs in several isoforms that can be distinguished by their isoelectric point. The low isoelectric point (4.5) isoforms of tyrosinase from the sporophores of A. bisporus U1 appeared to be glycoproteins. About 50% of their activity was retained on Concanavalin-A-Sepharose. Isoelectric focusing followed by staining for activity and glycoproteins indicated a glycoprotein with the same chromatographic behaviour as tyrosinase. Of the total tyrosinase activity, 5-12% occurred in the low isoelectric point form; of this fraction, 74% appears to be glycosylated, corresponding to 8% of total tyrosinase activity in the sporophore.

引用

页码：573 / 577

页数：5

共 19 条

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[2]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[3] IDENTIFICATION OF TYROSINASE IN MUSHROOMS BY ISOELECTRIC-FOCUSING [J].