Molecular analysis of allergenic proteins in bovine dander.
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.
Rautiainen
J
J
Department of Clinical Microbiology, University of Kuopio, Finland.
Pentikäinen
J
J
Rytkönen
M
M
Linnala-Kankkunen
A
A
Pelkonen
J
J
Virtanen
T
T
Mäntyjärvi
R
R
D000485:Allergens / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D011506:Proteins / Q000032:analysis*; D012867:Skin / Q000276:immunology*
D000485:Allergens; D011506:Proteins