Abstract
The respiratory burst oxidase of human neutrophils was purified by "dye-affinity" chromatography over a red agarose column. Electrophoresis of the purified enzyme on NaDodSO4 gel showed a single major band at 64,000-66,000 daltons, together with some minor contaminants. On a nondenaturing gel, the enzyme ran as two closely spaced bands, the faster of which contained flavin. When these two bands were rerun separately on a NaDodSO4 gel, they gave identical patterns, each showing a major band at ca. 65,000 daltons. The specific activity (mean +/- SEM) of the purified enzyme was 8.8 +/- 3.5 mumol of O-2 per min/mg of protein.