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 language | English (US) |
|---|---|
| Pages (from-to) | 743-751 |
| Number of pages | 9 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 98 |
| Issue number | 3 |
| DOIs | |
| State | Published - Feb 12 1981 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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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. / Nakamura, Michio; Baxter, Charles R.; Masters, Bettie Sue S.
In: Biochemical and Biophysical Research Communications, Vol. 98, No. 3, 12.02.1981, p. 743-751.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Simultaneous demonstration of phagocytosis-connected oxygen consumption and corresponding NAD(P)H oxidase activity
T2 - Direct evidence for NADPH as the predominant electron donor to oxygen in phagocytizing human neutrophils
AU - Nakamura, Michio
AU - Baxter, Charles R.
AU - Masters, Bettie Sue S
PY - 1981/2/12
Y1 - 1981/2/12
N2 - 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.
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.
UR - http://www.scopus.com/inward/record.url?scp=0019522689&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0019522689&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(81)91175-X
DO - 10.1016/0006-291X(81)91175-X
M3 - Article
C2 - 7225119
AN - SCOPUS:0019522689
VL - 98
SP - 743
EP - 751
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -