Linked Life Data

7649410

Source:http://linkedlifedata.com/resource/pubmed/id/7649410

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1995-9-25
pubmed:abstractText
Although radioiodinated interleukin 2 (IL-2) has been used to define the binding characteristics of the cytokine to the alpha chain of the receptor complex, we have found that unsubstituted IL-2 behaves differently. Whereas previous investigations with radioiodinated IL-2 have shown binding to the alpha chain with a Kd of 10 nM, we show that unsubstituted IL-2 binds to the alpha chain but does not reach saturation between 100 and 1000 nM. The explanation for the discrepancy between the analysis of radioiodinated and unsubstituted cytokine involves the propensity of unsubstituted IL-2 for self-association, a property that is abrogated by radioiodination. The functional relevance of our findings is indicated by the different capacities of unsubstituted and iodinated cytokine to induce prolonged proliferation of human T lymphocytes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0892-6638
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1096-102
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Self-association of interleukin 2 bound to its receptor.
pubmed:affiliation
Department of Pathology, Case Western Reserve University, Cleveland, Ohio 44106, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.