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Molecular analysis of allergenic proteins in bovine dander
Author(s) -
Rautiainen J.,
Pentikäinen J.,
Rytkönen M.,
LinnalaKankkunen A.,
Pelkonen J.,
Virtanen T.,
Mäntyjärvi R.
Publication year - 1996
Publication title -
allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.363
H-Index - 173
eISSN - 1398-9995
pISSN - 0105-4538
DOI - 10.1111/j.1398-9995.1996.tb04633.x
Subject(s) - allergen , size exclusion chromatography , dander , chemistry , biochemistry , microbiology and biotechnology , biology , allergy , immunology , enzyme
An analytic procedure was established to characterize bovine dander proteins with allergenic properties. The proteins from dander extract were separated by size‐exclusion gel filtration, and the fractions were studied with SDS‐PAGE followed by immunoblotting. An 11‐kDa allergen was found in the same gel filtration fractions as 20‐ and 22‐kDa allergens, and this suggests that the 11‐kDa allergen is a dimer in its native form. Our method also detected two separate 22‐kDa allergens. The primary structure of the major bovine dander allergen (BDA20) was also studied. A protein sequencer was used to determine the amino acid sequences of enzymatically cleaved peptides. The homology searches revealed that BDA20 is not a previously known bovine protein.