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pubmed-article:7594639pubmed:abstractTextImmunoscreening 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.lld:pubmed
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pubmed-article:7594639pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:7594639pubmed:articleTitlecDNA cloning and protein analysis of a bovine dermal allergen with homology to psoriasin.lld:pubmed
pubmed-article:7594639pubmed:affiliationDepartment of Clinical Microbiology, University of Kuopio, Finland.lld:pubmed
pubmed-article:7594639pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7594639pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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