| Autor: |
Lombardero M; Research Department, Alergia e Inmunología Abelló SA, Madrid, Spain., Quirce S, Duffort O, Barber D, Carpizo J, Chamorro MJ, Lezaun A, Carreira J |
| Jazyk: |
angličtina |
| Zdroj: |
The Journal of allergy and clinical immunology [J Allergy Clin Immunol] 1992 Apr; Vol. 89 (4), pp. 884-94. |
| DOI: |
10.1016/0091-6749(92)90445-8 |
| Abstrakt: |
Several monoclonal antibodies (MAbs) were raised against Olea europaea pollen-extract components. Two of these antibodies, named OL 2 and OL 7, recognize two nonoverlapping, nonrepeating epitopes on the olive-allergen Ole e I, as demonstrated by different techniques. The allergen was purified in a single step by MAb-based affinity chromatography, and the allergen revealed a band at molecular weight 20 kd as well as a minor band at 18 kd on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The contribution of allergen Ole e I to the allergenic activity of O. europaea pollen extracts was determined from the effect of allergen depletion by affinity chromatography on skin reactivity and a histamine-release test. The removal of allergen caused a large reduction in the activity of the preparation in 25 monospecific olive-allergic patients. In agreement, the affinity-purified allergen demonstrated a similar response when it was compared with the whole extract in these assays. The results indicated that Ole e I is by far the most important olive-pollen allergen. A two-site solid-phase radioimmunoassay was developed for the quantitation of the allergen Ole e I in mass units. The assay was based on the MAbs, OL 2 and OL 7, and had a detection limit in the nanogram range. A good correlation was found between allergenic activity, as determined by RAST inhibition, and allergen content in 18 olive-pollen extracts. This result indicates that the assay can be a good alternative to RAST inhibition for the standardization of O. europaea extracts. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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