Linked Life Data

9544808

Source:http://linkedlifedata.com/resource/pubmed/id/9544808

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-5-15
pubmed:abstractText
Cod fish is one of the foods most frequently involved in allergy. Only the cod allergen Gad c I, a 12.3 kDa parvalbumin, has been purified and characterized. Recently, we have detected allergen bands which have not previously been described, in particular a 41 kDa protein, by Western-blot. In the present work, this protein has been purified from a crude cod extract by ammonium sulfate fractionation, hydroxyapatite chromatography and preparative electrophoresis; a single band with an Mr of 41 x 10(3) was found in silver-stained sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The amino acid composition and the isoelectric point of the protein were determined. The purified protein (p41) was shown to bind specifically to reaginic IgE from sera of cod-allergic individuals and to a monoclonal anti-parvalbumin which recognizes specifically the first calcium binding site of parvalbumins. p41 may therefore contain a calcium binding site corresponding to an IgE-epitope similar to that of Gad c I.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1387-2273
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
706
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
63-71
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Purification of a 41 kDa cod-allergenic protein.
pubmed:affiliation
Laboratoire de Pathologie Cellulaire et Moléculaire en Nutrition, EP CNRS 0616, Faculté de Médecine, Vandoeuvre-lès-Nancy, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't