Linked Life Data

8392946

Source:http://linkedlifedata.com/resource/pubmed/id/8392946

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-8-24
pubmed:abstractText
Purified cytochrome b559 from guinea pig macrophages was relipidated with several phospholipid mixtures. Relipidated cytochrome b559 was found capable of NADPH-dependent superoxide (O2-) production in the absence of the cytosolic components of the NADPH oxidase complex. The rate of O2- generation by cytochrome b559 varied with the type of phospholipid utilized for relipidation, was absolutely dependent on exogenous FAD, and was enhanced by a critical concentration of anionic amphiphile. It is demonstrated that exogenous FAD acts by binding to cytochrome b559. These results provide firm experimental evidence for the proposal that cytochrome b559 comprises the complete electron transporting apparatus of the O2- forming NADPH oxidase and that the cytosolic components function merely as activators.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
327
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
57-62
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Generation of superoxide by purified and relipidated cytochrome b559 in the absence of cytosolic activators.
pubmed:affiliation
Department of Human Microbiology, Sackler School of Medicine, Tel-Aviv University, Israel.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't