Linked Life Data

6477562

Source:http://linkedlifedata.com/resource/pubmed/id/6477562

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1984-10-3
pubmed:abstractText
The oxidation state of Cu,Zn superoxide dismutase was investigated by 19F-NMR spectroscopy in intact red blood cells and in their lysates. The superoxide dismutase concentration was determined in the red cells both by activity and by F- nuclear relaxation rate measurements and the results obtained showed that the high relaxation rate of F- in erythrocytes is mainly due to the presence of superoxide dismutase. The relaxation rate of F- was unaffected or slightly increased by the addition of a superoxide ion generating system to the cells or to their lysates so indicating that superoxide dismutase is fundamentally in steady state. The results are discussed in terms of the possible reactions of the enzyme in erythrocytes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
122
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1276-81
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
An NMR study of the oxidation state of Cu,Zn superoxide dismutase in human red blood cells.
pubmed:publicationType
Journal Article