Molecular analysis of allergenic proteins in bovine dander.

Rautiainen, J; Pentikäinen, J; Rytkönen, M; Linnala-Kankkunen, A; Pelkonen, J; Virtanen, T; Mäntyjärvi, R · Allergy · 1996

basic_science · Level V

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Abstract

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.

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