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Characterization of two monoclonal antibodies against cytochrome b558 of
human neutrophils
AJ Verhoeven, BG Bolscher, LJ Meerhof, R van Zwieten, J Keijer, RS Weening and D Roos
Central Laboratory, The Netherlands Red Cross Blood Transfusion Service,
Amsterdam.
Monoclonal antibodies (MoAbs) were raised against cytochrome b558, a
membrane-bound component of the NADPH:O2 oxidoreductase in human
neutrophils. This cytochrome consists of a low-molecular-weight (low-
mol-wt) subunit of 22 to 23 Kd, probably encoded by an autosomal gene, and
a high-mol-wt subunit of 75 to 90 Kd, encoded on the X-chromosome. MoAb 449
reacts with the low-mol-wt subunit and MoAb 48 with the high- mol-wt
subunit on Western blots of purified cytochrome b558 and on blots of whole
neutrophil extracts. In extracts of neutrophils from patients with chronic
granulomatous disease (CGD) in which cytochrome b558 is not detectable by
spectrophotometric methods, the low-mol-wt subunit is present, albeit in a
much smaller amount. The high-mol-wt subunit is not detected by MoAb 48 in
neutrophils of patients with X- linked CGD and in neutrophils of patients
with the autosomal, cytochrome-b558-negative form of the disease. These
results can be explained by a marked instability of these subunits when the
synthesis of either of the two is disturbed. In differentiated HL-60 cells,
the high-mol-wt subunit appears to be present in a different form. Cloning
of the low-mol-wt subunit with the help of MoAb 449 suggests the presence
of a heme-binding site on this subunit. By comparison of the binding
characteristics of MoAb 449 to intact and permeabilized neutrophils with
those of MoAb 7D5, recently isolated by Nakamura et al (Blood 69:1404,
1987), the low-mol-wt subunit was established as a transmembrane protein.
Volume 73,
Issue 6,
pp. 1686-1694,
05/01/1989
Copyright © 1989 by The American Society of Hematology
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