Linked Life Data

1692814

Source:http://linkedlifedata.com/resource/pubmed/id/1692814

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-6-28
pubmed:abstractText
The antigenic and allergenic epitope maps of the hen egg-white ovalbumin, ovomucoid, ovotransferrin and lysozyme were obtained using one-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis and two-dimensional sodium dodecyl sulfate gel electrophoresis following isoelectric focusing. The isoelectric points of egg-white proteins were assigned by the isoelectric focusing technique. Two-dimensional electrophoresis following isoelectric focusing provided further information regarding epitope mapping. Furthermore, electrophoretic transfer of the proteins to nitrocellulose and subsequent immunoautoradiography, clearly demonstrated the allergenicity of these proteins. An important benefit of these methods was confirming that lysozyme bound strongly to IgE in all the human sera from egg-allergic individuals and that lysozyme, in addition to ovalbumin, ovomucoid and ovotransferrin, was one of the major allergens of hen egg-white.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0020-5915
pubmed:author
pubmed:issnType
Print
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
136-41
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Characterization of four major allergens of hen egg-white by IEF/SDS-PAGE combined with electrophoretic transfer and IgE-immunoautoradiography.
pubmed:affiliation
Laboratory of Clinical Biochemistry, University Hospital, Bergen, Norway.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't