Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1977-3-15
pubmed:abstractText
The cell surface component (receptor) which specifically binds immunoglobulin E (IgE) presumably forms an integral part of the functional chain involved in the antigen-induced IgE-mediated degranulation of histamine-containing mast cells and basophils. This paper describes a simple (NH4)2SO4 predipitation assay with which the interaction of IgE with detergent-solubilized receptors can be reproducibly quantitated. Receptor saturation was demonstrated and a linear response to receptor concentration over at least a 30-fold rang obtained. By means of the assay it was shown that (a) all assayable receptors of rat basophil leukemia cells are cell surface expressed; (b) receptor specificity remains intact during solubilization; (c) the binding constants of the solubilized IgE receptors are similar to those determined on intact cells. Utilizing agarose gel filtration, preliminary estimates of the molecular weight of the active free solubilized receptor and of its complex with IgE suggest that the receptor is univalent.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
252
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
704-11
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Assay and partial characterization of the solubilized cell surface receptor for immunoglobulin E.
pubmed:publicationType
Journal Article