Linked Life Data

1643437

Source:http://linkedlifedata.com/resource/pubmed/id/1643437

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-9-10
pubmed:abstractText
Timothy pollen extract was separated by 2D PAGE blot for further characterization of the major allergen Phl p V. Using pooled patient serum, we demonstrated that Phl p V consists of 4 components at 32 kD and 4 components at 38 kD, each differing in their pIs. The primary structure and the amino acid composition of the 8 proteins were determined form the blotted samples. Proteins of the same molecular weight did not differ in the 20 N-terminal amino acid residues, whereas the 32- and 38-kD proteins showed only 60% sequence identity. Furthermore, the results of the amino acid analyses suggest differences in their protein structure. Therefore, it might be possible that both proteins express different IgE-reactive epitopes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1018-2438
pubmed:author
pubmed:issnType
Print
pubmed:volume
98
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
105-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Characterization of isoforms of the major allergen Phl p V by two-dimensional immunoblotting and microsequencing.
pubmed:affiliation
Division of Allergology, Forschungsinstitut Borstel, FRG.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't