Linked Life Data

9178938

Source:http://linkedlifedata.com/resource/pubmed/id/9178938

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1997-7-31
pubmed:abstractText
125I-Labeled recombinant human neuron-specific enolase (R-NSE) was inadequate for RIA as a labeled antigen. The binding activity of labeled R-NSE to the antibody was markedly decreased. To supplement this defect and facilitate purification, we constructed two R-NSE derivatives, Y-NSE (one tyrosine residue was added at the N-terminal of R-NSE) and Y-NSE.H6 (six histidine residues were further added at the C-terminal of Y-NSE). The biochemical and immunochemical characteristics of these R-NSE derivatives were essentially the same to those of R-NSE. These derivatives were useful not only as standards for enzyme immunoassay (EIA), but also as labeled antigens for RIA. These results clearly indicate that the reactivity of these modified NSEs to anti-NSE antibody is almost equivalent to that of human brain gammagamma-enolase (B-NSE), and that even if the modified NSEs are labeled, they retain their binding affinities to antibodies in contrast to R-NSE.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0918-6158
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
556-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Biochemical and immunochemical properties of modified human neuron-specific enolase.
pubmed:affiliation
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Health Sciences University of Hokkaido, Ishikari-Tobetsu, Japan.
pubmed:publicationType
Journal Article, Comparative Study