Linked Life Data

2026245

Source:http://linkedlifedata.com/resource/pubmed/id/2026245

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-6-12
pubmed:abstractText
Murine monoclonal antibodies directed against a native form of Cu, Zn-superoxide dismutase (SOD) were produced by immunizing SOD purified from human erythrocytes. The monoclonal antibodies able to bind SOD were further screened for their ability to absorb SOD activity using anti-mouse IgG conjugated iron beads as solid supports in magnetic separation. This new screening method revealed the heterogeneity of native SOD in the reactivity with the antibodies. One monoclonal antibody successfully absorbed the entire activity of SOD detected by an inhibition assay of cypridina luciferin analog (MCLA)-dependent chemiluminescence induced by superoxide anion production, while other absorbed only a part of the SOD activity. The evidence that all of the latter antibodies failed to react with recombinant artificial SOD free of charge isomers suggested correlation of the heterogeneity with the presence of charge isomeric forms. The former antibody was further used to establish a fluorescence sandwich enzyme immunoassay, and this assay provided a very sensitive detection limit as low as 100 pg/ml.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
282
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
115-8
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Detection of heterogeneity of Cu, Zn-superoxide dismutase with monoclonal antibodies and the establishment of a highly sensitive fluorescence sandwich enzyme-linked immunosorbent assay.
pubmed:affiliation
Third Department of Internal Medicine, Gunma University, Japan.
pubmed:publicationType
Journal Article