Characterization of isoforms of the major allergen Phl p V by two-dimensional immunoblotting and microsequencing.
Timothy pollen extract was separated by 2D PAGE blot for further characterization of the major allergen Phl p V. Using pooled patient serum, we demonstrated that Phl p V consists of 4 components at 32 kD and 4 components at 38 kD, each differing in their pIs. The primary structure and the amino acid composition of the 8 proteins were determined form the blotted samples. Proteins of the same molecular weight did not differ in the 20 N-terminal amino acid residues, whereas the 32- and 38-kD proteins showed only 60% sequence identity. Furthermore, the results of the amino acid analyses suggest differences in their protein structure. Therefore, it might be possible that both proteins express different IgE-reactive epitopes.
Petersen
A
A
Division of Allergology, Forschungsinstitut Borstel, FRG.
Becker
W M
WM
Schlaak
M
M
D000485:Allergens / Q000737:chemistry* / Q000276:immunology; D000595:Amino Acid Sequence; D015180:Electrophoresis, Gel, Two-Dimensional; D006801:Humans; D015151:Immunoblotting; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry / Q000276:immunology*; D006109:Poaceae / Q000276:immunology*; D011058:Pollen / Q000737:chemistry / Q000276:immunology*
D000485:Allergens; C076049:Phl p V protein, Phleum pratense; D010940:Plant Proteins