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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1985 May;82(10):3144–3148. doi: 10.1073/pnas.82.10.3144

Respiratory burst oxidase from human neutrophils: purification and some properties.

M Markert, G A Glass, B M Babior
PMCID: PMC397731  PMID: 3858811

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.

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Selected References

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