Linked Life Data

2187495

Source:http://linkedlifedata.com/resource/pubmed/id/2187495

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1990-6-25
pubmed:abstractText
Interleukin-3 (IL-3) regulates the proliferation of myeloid, erythroid, and lymphoid cells. Previous reports showed IL-3 binding restricted to a single high-affinity (Kd = 50-200 pM) site. Here, we demonstrate by equilibrium studies an additional binding site for IL-3 with lower apparent affinity (Kd = 5-20 nM). Furthermore, kinetic analysis shows that two binding sites for IL-3 exist: IL-3 dissociates slowly from the first site (T1/2 = 4 hr; k-1 = 2.7 x 10(-3) min-1), whereas it dissociates rapidly (T1/2 = 4.0 min; k-1 = 0.116 min-1) from the second site. Cross-linking showed that [125I]IL-3 binding to the 115- and 140-kD proteins was not saturable at concentrations commensurate with high-affinity binding and IL-3 dissociated rapidly from these same molecules. Thus, the low affinity IL-3 receptor is a molecule(s) of 115- to 140-kD.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0897-7194
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
221-33
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Evidence for a low-affinity interleukin-3 receptor.
pubmed:affiliation
Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304-1104.
pubmed:publicationType
Journal Article