Two cytosolic components of the neutrophil NADPH oxidase, P47-PHOX and P67-PHOX, are not flavoproteins

Tsukasa Chiba, Mizuho Kaneda, Hirotada Fujii, Robert A. Clark, William M. Nauseef, Katsuko Kakinuma

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

Two cytosolic proteins, p47-phox and p67-phox, have been shown to be essential components of the NADPH-dependent oxidase of human neutrophils, although the specific role of each of these proteins in the multicomponent electron transport complex is undetermined. The superoxide-generating activity of this oxidase can be reproduced in a cell-free system, combining cytosol and membranes from unstimulated neutrophils in the presence of fatty acid and NADPH. In the present studies, cytosol was treated with myristic acid, arachidonic acid, or sodium dodecyl sulfate in the absence of membranes and the resultant precipitate collected by centrifugation and analyzed. Both p47-phox and p67-phox precipitated in the presence of fatty acid. However, neither FAD nor FMN was localized in the precipitates, even though substantial amounts of p47-phox and p67-phox precipitated. These results suggest that neither p47-phox nor p67-phox is a flavoprotein and that neither, therefore, is the oxidase component which accepts electrons from NADPH.

Original languageEnglish (US)
Pages (from-to)376-381
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume173
Issue number1
DOIs
StatePublished - Nov 30 1990
Externally publishedYes

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ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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