Linked Life Data

9686871

Source:http://linkedlifedata.com/resource/pubmed/id/9686871

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1998-9-30
pubmed:abstractText
Purification of two allergens from horse (Equus caballus) sweat, Equ c2 and Equ c3, by means of salt-promoted chromatography on a "thiophilic" (T-gel) adsorbent is described. Immobilization of these proteins was found to be dependent on the presence of water-structure-forming salts where the ammonium sulphate concentration in the equilibration buffer was 2 M. Equ c2 showed higher affinity towards the thiophilic matrix than Equ c3. Their molecular mass (Mr) values established by SDS-polyacrylamide gel electrophoresis were for Equ c2 approximately 17,000 and for Equ c3 approximately 16,000, and both proteins showed a low isoelectric point of approximately 3.8. Their allergenic properties were also investigated using sera from horse-sensitized patients, where it was demonstrated that these proteins exhibited an IgE antibody binding capacity. In this report we show the broad potential applications of thiophilic adsorption chromatography for the efficient purification of allergens.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1387-2273
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
710
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
57-65
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Thiophilic adsorption chromatography: purification of Equ c2 and Equ c3, two horse allergens from horse sweat.
pubmed:affiliation
Unité d'Immuno-Allergie, Département de Physiopathologie, Institut Pasteur, Paris, France.
pubmed:publicationType
Journal Article