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Porcine polymorphonuclear leukocyte NADPH-cytochrome c reductase generates superoxide in the presence of cytochrome b559 and phospholipid
- Source :
- Biochemical and Biophysical Research Communications. 147:71-77
- Publication Year :
- 1987
- Publisher :
- Elsevier BV, 1987.
-
Abstract
- NADPH-cytochrome c reductase and cytochrome b559 were purified from the membrane fraction of phorbol myristate acetate-stimulated porcine polymorphonuclear leukocytes. The highly purified reductase oxidized NADPH and generated superoxide when combined with partially purified cytochrome b559 in the presence of phosphatidylcholine. In the same system, but under the anaerobic condition, the reductase was found to reduce cytochrome b559.
- Subjects :
- Neutrophils
Swine
Biophysics
Phospholipid
Cytochrome b559
Reductase
Biochemistry
chemistry.chemical_compound
Superoxides
Animals
Cytochrome c oxidase
Molecular Biology
NADPH-Ferrihemoprotein Reductase
biology
Superoxide
Cytochrome c
Photosystem II Protein Complex
Cytochrome P450 reductase
Cell Biology
Cytochrome b Group
Molecular biology
chemistry
Phosphatidylcholines
biology.protein
Phorbol
Oxidation-Reduction
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 147
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....20851b00dca4e90ca6edc27c3b72ab11
- Full Text :
- https://doi.org/10.1016/s0006-291x(87)80088-8