Purification and fine characterization of a major allergen from Olea europaea pollen extract |
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| Authors: | F. De Cesare C. Pini G. Di Felice M. F. Caiaffa L. Macchia A. Tursi R. Tinghino S. Palumbo F. Sallusto R. Federico |
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| Affiliation: | Department of Plant Biology, University "La Sapienza", Rome, Italy;Department of Allergology and Clinical Immunology, University of Bari, Rome, Italy;Department of Immunology, Istituto Superiore di Sanità, Rome, Italy |
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| Abstract: | ![]()
Olea europaea (olive) pollen extract was prepared by aqueous extraction and characterized by biochemical and immunochemical methods. Two components, displaying respective mol. wt. of 17000 and 19000, were the most reactive allergens, being the doublet (designated Ole e I) recognized by most sera tested. The 19000 mol. wt. component, purified by conventional biochemical procedure and lectin-affinity chromatography from the Ole e I doublet, was deglycosylated and analyzed by SDS–PAGE and by ELISA inhibition. The results obtained suggest that the 19000 mol. wt. component represents the glycosylated form of the 17000 component. |
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| Keywords: | allergen purification chemical deglycosylation ELISA IgE Olea europaea SDS–PAGE |
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