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D Choury, A Reghis, AL Pichard and JC Kaplan
The problem of the low activity of so-called methemoglobin reductase in red
cells from newborns was reinvestigated in view of our current knowledge of
this enzyme, i.e., (1) its being cytochrome-b5 reductase and (2) its
presence in two forms: soluble and membrane-bound. We found that red cells
from cord blood and newborns exhibited a 50% decrease of soluble
cytochrome-b5 reductase activity, whereas membrane-bound activity was in
the adult range. Ghosts from these cells possessed diminished ability to
solubilize membrane-bound cytochrome-b5 reductase in the course of in vitro
auto-incubation. This autosolubilizing ability increased with age and
reached adult level concomitantly with soluble cytochrome-b5 reductase
activity at 6 mo. We conclude that the relative deficiency of soluble
cytochrome-b5 reductase observed at birth is due to diminished
post-translational processing of the membrane-bound enzyme during
erythropoiesis of fetal cells. This processing is calcium-dependent related
to calmodulin.
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| Copyright © 1983 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||