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Research Article Free access | 10.1172/JCI118882

The cytosolic subunit p67phox contains an NADPH-binding site that participates in catalysis by the leukocyte NADPH oxidase.

R M Smith, J A Connor, L M Chen, and B M Babior

The Department of Medicine, University of California, San Diego 92093, USA.

Find articles by Smith, R. in: PubMed | Google Scholar

The Department of Medicine, University of California, San Diego 92093, USA.

Find articles by Connor, J. in: PubMed | Google Scholar

The Department of Medicine, University of California, San Diego 92093, USA.

Find articles by Chen, L. in: PubMed | Google Scholar

The Department of Medicine, University of California, San Diego 92093, USA.

Find articles by Babior, B. in: PubMed | Google Scholar

Published August 15, 1996 - More info

Published in Volume 98, Issue 4 on August 15, 1996
J Clin Invest. 1996;98(4):977–983. https://doi.org/10.1172/JCI118882.
© 1996 The American Society for Clinical Investigation
Published August 15, 1996 - Version history
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Abstract

The NADPH-dependent respiratory burst oxidase of human neutrophils catalyzes the reduction of oxygen to superoxide using NADPH as the electron donor and is essential for normal host defenses. To gain insight into the function of the various oxidase subunits that are required for the full expression of catalytic activity, we studied the interactions between the 2',3'-dialdehyde derivative of NADPH (NADPH dialdehyde) and neutrophil cytosol. NADPH dialdehyde treatment of cytosol resulted in the loss of the ability of the cytosol to participate in cell-free oxidase activation; this inactivation was blocked by NADPH but not by NAD, NADP, or GTP. Partial purification of neutrophil cytosol yielded a single peak which could restore the activity lost in cytosol treated with NADPH dialdehyde. This peak contained p67phox but not p47phox or Rac2. Purified recombinant p67phox was similarly able to restore the activity lost in NADPH dialdehyde-treated cytosol and bound [32P]NADPH dialdehyde in a specific fashion. The activity of recombinant p67phox in cell-free oxidase assays was lost on treatment with NADPH dialdehyde. Together, these data suggest p67phox contains the catalytic NADPH-binding site of the leukocyte NADPH oxidase.

Version history
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