Linked Life Data

3083239

Source:http://linkedlifedata.com/resource/pubmed/id/3083239

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1986-4-28
pubmed:abstractText
Membrane immunoglobulin receptors on chicken B-cells have been shown to display a heterogeneity with respect to interchain disulfide linkages. One fraction of the surface Ig (sIg) appears to display the traditional H2-L2 linkage. We also present evidence that this Ig is covalently bound via a disulfide linkage to actin. In this instance, the isolated Ig heavy chain, after reduction, has a mol. wt of 80 K. Perhaps more significantly, we show that another fraction of the sIg exists in a highly aggregated from that is stabilized by disulfide linkages. In contrast to the sIg found in the H2-L2 configuration, there is no evidence of actin within the aggregates and the sIg heavy chains isolated from these aggregates display a slightly faster mobility on SDS-PAGE under reducing conditions, running at about 77K. Furthermore, it appears that the Ig within the large aggregates may have a higher avidity with respect to antigen binding, and so this Ig structure may be the more relevant to antigen-induced receptor-mediated signaling in the B-cell.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0161-5890
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-13
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Disulfide linkages between antigen-binding receptors on chicken B-lymphocytes.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.