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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1995-12-8
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pubmed:databankReference |
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pubmed:abstractText |
Immunoscreening of a cDNA library from bovine skin led to isolation of clones coding for an allergen named BDA11. Sequence analysis of the clones revealed that they can encode a protein of 11.6 kDa with a predicted pI of 5.19. Allergenicity of BDA11 was verified by the IgE reactivity in cattle-allergic patients' sera with the recombinant protein produced in Escherichia coli. A biochemically purified native allergen of 11 kDa from bovine dander was identified as BDA11 by peptide sequencing. Homology comparisons showed that BDA11 had a 63.4% amino acid identity with human psoriasin. Psoriasin is a calcium-binding protein expressed in keratinocytes, and it is strongly up-regulated in psoriatic skin. BDA11 also had segments homologous with calcium-binding proteins from three other species.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-202X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
105
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
660-3
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7594639-Allergens,
pubmed-meshheading:7594639-Amino Acid Sequence,
pubmed-meshheading:7594639-Animals,
pubmed-meshheading:7594639-Base Sequence,
pubmed-meshheading:7594639-Calcium-Binding Proteins,
pubmed-meshheading:7594639-Cattle,
pubmed-meshheading:7594639-Cloning, Molecular,
pubmed-meshheading:7594639-DNA, Complementary,
pubmed-meshheading:7594639-Epitopes,
pubmed-meshheading:7594639-Gene Expression,
pubmed-meshheading:7594639-Humans,
pubmed-meshheading:7594639-Molecular Sequence Data,
pubmed-meshheading:7594639-Protein Structure, Secondary,
pubmed-meshheading:7594639-S100 Proteins,
pubmed-meshheading:7594639-Sequence Homology, Amino Acid,
pubmed-meshheading:7594639-Skin
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pubmed:year |
1995
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pubmed:articleTitle |
cDNA cloning and protein analysis of a bovine dermal allergen with homology to psoriasin.
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pubmed:affiliation |
Department of Clinical Microbiology, University of Kuopio, Finland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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