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Superoxide-forming enzyme from human neutrophils: evidence for a flavin requirement
Open accessAbstract
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 micron flavin adenine dinucleotide (FAD), but not by flavin mononucleotide, riboflavin, adenosine 5′-diphosphate, or adenosine 5′-monophosphate. 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. These results suggest that the superoxide-forming enzyme from human neutrophils is a FAD-requiring enzyme.
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“NOX2 is predominantly expressed in phagocytes and produces a relatively large amount of superoxide in order to kill bacteria within phagosomes in an inflamed area [33,34], Figure 13.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [33]
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“The transmembrane domain includes four conserved histidines that serve as binding sites for two heme moieties bound between helices III and V (288, 613), and the flavoprotein domain binds the cofactor FAD and includes a binding site for NADPH (49, 480, 613, 980).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [49]
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Metadata
- Authors
- Babior, B., & Kipnes, R.
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 1977-09-01
- Volume
- 50
- Issue
- 3
- Pages
- 517-524
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W2475048516
- Cited by
- 174
- References
- 23
- Citations by year
- 2023: 4 · 2022: 2 · 2021: 2 · 2019: 3 · 2018: 1 · 2016: 1 · 2014: 2 · 2013: 1
- FWCI
- 2.86
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Blood (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Keywords
- neutrophils, flavin adenine dinucleotide, NADPH oxidase, zymosan, chronic granulomatous disease, detergent extraction, Triton X-100, flavin mononucleotide, riboflavin
- MeSH terms
- Adenine Nucleotides, Detergents, Flavins, Granulomatous Disease, Chronic, Humans, Neutrophils, Peroxides, Zymosan
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