Basic isoforms of Par o 1, the major allergen of Parietaria officinalis pollen.
We describe a group of basic isoforms of Par o 1 (cumulatively referred to as Par o 1b), purified by anion-exchange chromatography. The allergenic activity of Par o 1b was compared with that of the acidic isoform (Par o 1a) by RAST inhibition. Par o 1b showed a cathodic mobility in crossed immunoelectrophoresis. It was found to be homogeneous in SDS-PAGE and SE-HPLC (14.5 kDa), and heterogeneous in PAG-IEF, yielding five IgE-binding bands with pI ranging between 7.9 and 9.6 PAG-IEF individual components were isolated by cation-exchange HPLC. The N-terminal amino acid sequence of the main component (pI 8.8) was determined and found to be similar to that of Par o 1a.
Coscia
M R
MR
Institute of Protein Biochemistry and Enzymology, CNR, Naples, Italy.
Ruffilli
A
A
Oreste
U
U
D000485:Allergens / Q000032:analysis* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007122:Immunoelectrophoresis; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry; D011058:Pollen / Q000737:chemistry*; D011852:Radioallergosorbent Test
D000485:Allergens; D010940:Plant Proteins