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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1997-3-19
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pubmed:abstractText |
The major birch (Betula alba L.) pollen allergen, Bet v 1, has been shown to be homologous to pathogenesis-related proteins in a number of plants. Recently, it was demonstrated that a ginseng protein with high homology to an intracellular pathogenesis-related protein of parsley and to Bet v 1 is a ribonuclease (RNase). Birch pollen extract was separated in an RNase activity gel. Four major RNase bands were excised from the gel, reseparated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and identified by Western blotting with a specific Bet v 1 monoclonal antibody and patient's serum. Thus the monomer and the dimer of Bet v 1 showed RNase activity. Purified recombinant Bet v 1 was shown to degrade plant RNA. The RNase activity of recombinant Bet v 1 was 180 units.mg-1.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
B
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Allergens,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Bet v 1 allergen, Betula,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases
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pubmed:status |
MEDLINE
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pubmed:issn |
0032-0935
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
199
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
413-5
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pubmed:dateRevised |
2011-6-21
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pubmed:meshHeading |
pubmed-meshheading:8771801-Allergens,
pubmed-meshheading:8771801-Amino Acid Sequence,
pubmed-meshheading:8771801-Antigens, Plant,
pubmed-meshheading:8771801-Molecular Sequence Data,
pubmed-meshheading:8771801-Plant Proteins,
pubmed-meshheading:8771801-Pollen,
pubmed-meshheading:8771801-Ribonucleases,
pubmed-meshheading:8771801-Sequence Homology, Amino Acid,
pubmed-meshheading:8771801-Trees
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pubmed:year |
1996
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pubmed:articleTitle |
The major birch pollen allergen, Bet v 1, shows ribonuclease activity.
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pubmed:affiliation |
Research Center Borstel, Germany.
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pubmed:publicationType |
Journal Article
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