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Basic isoforms of Par o 1, the major allergen of Parietaria officinalis pollen
Author(s) -
Coscia M. R.,
Ruffilli A.,
Oreste U.
Publication year - 1995
Publication title -
allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.363
H-Index - 173
eISSN - 1398-9995
pISSN - 0105-4538
DOI - 10.1111/j.1398-9995.1995.tb02496.x
Subject(s) - allergen , isoelectric focusing , chemistry , gene isoform , high performance liquid chromatography , chromatography , venom , ion chromatography , immunoelectrophoresis , amino acid , biochemistry , biology , allergy , antigen , enzyme , immunology , gene
We describe a group of basic isoforms of Par o 1 (cumulatively referred to as Par o lb), purified by anion‐exchange chromatography. The allergenic activity of Par o lb was compared with that of the acidic isoform (Par o la) by RAST inhibition. Par o lb 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 la.