Simultaneous demonstration of phagocytosis-connected oxygen consumption and corresponding NAD(P)H oxidase activity: Direct evidence for NADPH as the predominant electron donor to oxygen in phagocytizing human neutrophils

Michio Nakamura, Charles R. Baxter, Bettie Sue S Masters

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30 Citations (Scopus)

Abstract

Phagocytosis-connected oxygen consumption by human neutrophils and corresponding NAD(P)H oxidase were measured by an oxygen electrode with sequential additions of opsonized zymosan, Renex 30 (0.067%), and NAD(P)H. At a concentration of 0.15 mM substrate, NADPH oxidase activity of stimulated neutrophils was twice that required to account for accompanying oxygen consumption, and was about 20 times higher than that activity obtained from resting cells. NADH oxidase activity of phagocytizing cells, however, was negligible at the same concentration of substrate. With high recovery of oxidase activity, these results strongly suggest that NADPH is the dominant electron donor to oxygen in phagocytizing human neutrophils.

Original languageEnglish (US)
Pages (from-to)743-751
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume98
Issue number3
DOIs
StatePublished - Feb 12 1981
Externally publishedYes

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NADPH Oxidase
NADP
Phagocytosis
Oxygen Consumption
Neutrophils
Demonstrations
Electrons
Oxygen
Zymosan
NAD
Oxidoreductases
Electrodes
Substrates
Cells
Recovery

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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title = "Simultaneous demonstration of phagocytosis-connected oxygen consumption and corresponding NAD(P)H oxidase activity: Direct evidence for NADPH as the predominant electron donor to oxygen in phagocytizing human neutrophils",
abstract = "Phagocytosis-connected oxygen consumption by human neutrophils and corresponding NAD(P)H oxidase were measured by an oxygen electrode with sequential additions of opsonized zymosan, Renex 30 (0.067{\%}), and NAD(P)H. At a concentration of 0.15 mM substrate, NADPH oxidase activity of stimulated neutrophils was twice that required to account for accompanying oxygen consumption, and was about 20 times higher than that activity obtained from resting cells. NADH oxidase activity of phagocytizing cells, however, was negligible at the same concentration of substrate. With high recovery of oxidase activity, these results strongly suggest that NADPH is the dominant electron donor to oxygen in phagocytizing human neutrophils.",
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T1 - Simultaneous demonstration of phagocytosis-connected oxygen consumption and corresponding NAD(P)H oxidase activity

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AU - Baxter, Charles R.

AU - Masters, Bettie Sue S

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AB - Phagocytosis-connected oxygen consumption by human neutrophils and corresponding NAD(P)H oxidase were measured by an oxygen electrode with sequential additions of opsonized zymosan, Renex 30 (0.067%), and NAD(P)H. At a concentration of 0.15 mM substrate, NADPH oxidase activity of stimulated neutrophils was twice that required to account for accompanying oxygen consumption, and was about 20 times higher than that activity obtained from resting cells. NADH oxidase activity of phagocytizing cells, however, was negligible at the same concentration of substrate. With high recovery of oxidase activity, these results strongly suggest that NADPH is the dominant electron donor to oxygen in phagocytizing human neutrophils.

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