Analysis of glycosylation sites on gp91phox, the flavocytochrome of the NADPH oxidase, by site-directed mutagenesis and translation in vitro

被引：78

作者：

Wallach, TM ^{[1
]}

Segal, AW ^{[1
]}

机构：

[1] UNIV LONDON UNIV COLL,DEPT MED,LONDON WC1E 6JJ,ENGLAND

来源：

BIOCHEMICAL JOURNAL | 1997年 / 321卷

基金：

英国惠康基金;

关键词：

D O I：

10.1042/bj3210583

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：

Flavocytochrome b(558) of the NADPH oxidase which generates superoxide in phagocytic cells, is a alpha(1) beta(1) heterodimer of gp91phox and p22phox, which together form a membrane-spanning electron-transport chain that transfers electrons from NADPH in the cytosol to oxygen. The C-terminal portion of gp91phox is a member of the ferredoxin-NADP(+) reductase family of reductases. Little is known of the organization of the N-terminal section of this molecule, which is associated with the two haem structures. It is N-glycosylated, and site-directed mutagenesis has been used to eliminate the five potential N-linked glycosylation consensus sites. Mutated cDNAs were expressed in vitro. This approach provided evidence for glycosylation of residues Asn(131), Asn(148) and Asn(239), but not of Asn(96) and Asn(429).

引用

页码：583 / 585

页数：3

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