Flavocytochrome b558 of the NADPH oxidase which generates superoxide in phagocytic cells, is a α1β1 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 Asn131, Asn148 and Asn239, but not of Asn96 and Asn429.
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February 1997
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Research Article|
February 01 1997
Analysis of glycosylation sites on gp91phox, the flavocytochrome of the NADPH oxidase, by site-directed mutagenesis and translation in vitro
Timothy M. WALLACH;
Timothy M. WALLACH
1Department of Medicine, University College London, 5 University Street, London WC1E 6JJ, U.K.
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Anthony W. SEGAL
Anthony W. SEGAL
*
1Department of Medicine, University College London, 5 University Street, London WC1E 6JJ, U.K.
*To whom correspondence should be addressed.
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Publisher: Portland Press Ltd
Received:
November 18 1996
Revision Received:
December 06 1996
Accepted:
December 09 1996
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 1997
1997
Biochem J (1997) 321 (3): 583–585.
Article history
Received:
November 18 1996
Revision Received:
December 06 1996
Accepted:
December 09 1996
Citation
Timothy M. WALLACH, Anthony W. SEGAL; Analysis of glycosylation sites on gp91phox, the flavocytochrome of the NADPH oxidase, by site-directed mutagenesis and translation in vitro. Biochem J 1 February 1997; 321 (3): 583–585. doi: https://doi.org/10.1042/bj3210583
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