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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1980-7-22
|
| pubmed:abstractText |
Concanavalin A-binding (Con-A)-binding cell surface glycoproteins were isolated, via Con A-affinity chromatography, from Triton X-100-solubilized Chinese hamster ovary (CHO) cell plasma membranes. The Con A binding glycoproteins isolated in this manner displayed a significantly different profile on sodium dodecyl sulfate--polyacrylamide gels than did the Triton-soluble surface components, which were not retarded by the Con-A-Sepharose column. [125I]-Con A overlays of the pooled column fractions displayed on sodium dodecyl sulfate--polyacrylamide gel electro-phoresis (SDS-PAGE) demonstrated that there were virtually no Con A receptors associated with the unretarded peak released by the Con A-Sepharose column, whereas the material which was bound and specifically eluted from the Con A-Sepharose column with the sugar hapten alpha-methyl-D-mannopyranoside contained at least 15 prominent bands which bound [125I]-Con A. In order to produce monoclonal antibodies against various cell surface Con A receptors, Balb/c mice were immunized with the pooled Con A receptor fraction. Following immunization spleens were excised from the animals and single spleen cell suspensions were fused with mouse myeloma P3/X63-Ag8 cells. Numerous hybridoma clones were subsequently picked on the basis of their ability to secrete antibody which could bind to both live and glutaraldehyde-fixed CHO cells as well as to the Triton-soluble fraction isolated from the CHO plasma membrane fraction. Antibody from two of these clones was able to precipitate a single [125I]-labeled CHO surface component of approximately 265,000 daltons.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0091-7419
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
11
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
563-77
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:544930-Animals,
pubmed-meshheading:544930-Antibody Formation,
pubmed-meshheading:544930-Antigens, Surface,
pubmed-meshheading:544930-Cell Line,
pubmed-meshheading:544930-Cell Membrane,
pubmed-meshheading:544930-Chromatography, Affinity,
pubmed-meshheading:544930-Clone Cells,
pubmed-meshheading:544930-Concanavalin A,
pubmed-meshheading:544930-Cricetinae,
pubmed-meshheading:544930-Cricetulus,
pubmed-meshheading:544930-Female,
pubmed-meshheading:544930-Glycoproteins,
pubmed-meshheading:544930-Hybrid Cells,
pubmed-meshheading:544930-Membrane Proteins,
pubmed-meshheading:544930-Mice,
pubmed-meshheading:544930-Mice, Inbred BALB C,
pubmed-meshheading:544930-Molecular Weight,
pubmed-meshheading:544930-Ovary,
pubmed-meshheading:544930-Radioimmunoassay
|
| pubmed:year |
1979
|
| pubmed:articleTitle |
Production of monoclonal antibodies against a cell surface concanavalin A binding glycoprotein.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|