SUPEROXIDE-FORMING ENZYME FROM HUMAN NEUTROPHILS - EVIDENCE FOR A FLAVIN REQUIREMENT

  • 1 January 1977
    • journal article
    • research article
    • Vol. 50  (3) , 517-524
Abstract
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 .mu.M FAD, but not by FMN, riboflavin, ADP or AMP. 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. The superoxide-forming enzyme from human neutrophils is apparently a FAD-requiring enzyme.