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

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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Markert, M. Glass, G. A. Babior, B. M.
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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	10
Volume Number	82
Language	English
Publisher	National Academy of Sciences
Publisher Date	1985-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	NADH, NADPH Oxidoreductases Isolation & Purification NADPH Oxidase Neutrophils Enzymology Photosystem II Protein Complex Cell Membrane Cytochrome b Group Flavins Molecular Weight Metabolism Spectrum Analysis Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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