Superoxide-forming enzyme from human neutrophils: evidence for a flavin
requirement
BM Babior and RS Kipnes
The superoxide-forming activity of 27,000-g particles prepared from
homogenates of zymosan-treated human neutrophils is lost if the assay is
conducted in the presence of 0.045% Triton X-100. This loss in activity in
the presence of detergent is prevented by 40 micron flavin adenine
dinucleotide (FAD), but not by flavin mononucleotide, riboflavin, adenosine
5'-diphosphate, or adenosine 5'-monophosphate. With resting particles or
particles from zymosan-treated chronic granulomatous disease neutrophils,
no superoxide-forming activity is detectable even in the presence of FAD;
this is true whether or not detergent is present in the assay. Particles
extracted with detergent prior to assay are fully active if assayed in the
presence of FAD, but show little activity if FAD is omitted from the assay
mixture. These results suggest that the superoxide-forming enzyme from
human neutrophils is a FAD-requiring enzyme.
Volume 50,
Issue 3,
pp. 517-524,
09/01/1977
Copyright © 1977 by The American Society of Hematology
