Linked Life Data

2536695

Source:http://linkedlifedata.com/resource/pubmed/id/2536695

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1989-3-13
pubmed:abstractText
The 2',3'-dialdehyde of NADPH (NADPH dialdehyde) appears to act as an affinity label toward the respiratory burst oxidase of human neutrophils, inactivating the enzyme by attaching covalently to a residue at its NADPH-binding site. Although the oxidase in activated neutrophils is known to reside in the plasma membrane, our studies showed that in resting neutrophils the NADPH dialdehyde-sensitive component of the enzyme was located in the cytosol. These findings suggest that one of the steps in the activation of the respiratory burst oxidase is the transfer of its NADPH-binding component from the cytosol to the plasma membrane of the cell.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1958-62
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Affinity labeling of the cytosolic and membrane components of the respiratory burst oxidase by the 2',3'-dialdehyde derivative of NADPH. Evidence for a cytosolic location of the nucleotide-binding site in the resting cell.
pubmed:affiliation
Department of Basic and Clinical Research, Research Institute of Scripps Clinic, La Jolla, California 92037.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.