Two-dimensional gel electrophoretic analyses of Kentucky bluegrass and rye grass pollen allergens. Detection with a murine monoclonal anti-Poa p I antibody and amino terminal amino acid sequence of Poa p I allergen.
Allergenic extracts of Kentucky bluegrass (Poa pratensis) and rye grass (Lolium perenne) pollen were shown by 2-dimensional (2-D) gel electrophoresis to consist of several hundred protein components. The pollen extracts of the two related grasses had unique 2-D gel patterns. Two major grass pollen allergens, Poa p I and Lol p I, and their isoforms (i.e. isoallergens) were detected and localized on 2-D gels by immunoblotting with anti-Poa p I antibody mAb 60. Poa p I isoallergens were less acidic than Lol p I isoallergens. The relative proportion of four Poa p I isoallergens was (in decreasing pI): A, 13%; B, 37%; and D, 15%. The amino terminal amino acid sequences of the two major isoallergens of Poa p I were identical. However, the amino acid composition of these isoallergens showed enough differences to account for their charge differences. The amino terminal amino acid sequence of two major Poa p I isoallergens had a 70% homology in 20 amino acid overlap with the previously published amino terminal amino acid sequence of rye grass pollen allergen R-7.
Ekramoddoullah
A K
AK
Pacific Forestry Centre, Forestry Canada, Victoria.
D000485:Allergens; D000595:Amino Acid Sequence; D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional; D005260:Female; D015151:Immunoblotting; D008129:Lolium / Q000032:analysis*; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D010940:Plant Proteins; D011058:Pollen / Q000032:analysis*; D012689:Sequence Homology, Nucleic Acid
D000485:Allergens; D010940:Plant Proteins; C058089:Poa p I proteins, Poa pratensis