parietaria judaica/carbohydrate

Cross-reactivity between the different components in Parietaria judaica pollen extract has been investigated by polyclonal as well as monoclonal antibodies before and after chemical deglycosylation obtained by trifluoromethanesulphonic acid (TFMS) treatment of the extract. In western blotting a

We have isolated CD8+ alpha/beta T cells from the blood of atopic and healthy individuals which recognize a nonpeptide antigen present in an allergenic extract from Parietaria judaica pollen. This antigen appears to be a carbohydrate because it is resistant to proteinase K and alkaline digestion, is

To investigate the biological activity of P. judaica and P. officinalis allergen preparations, 36 Spanish patients were included in a biological standardization (BS) trial. For both species the concentration corresponding to 1000 biological units/ml (BU/ml) was found to be about 2 micrograms dry

The main allergen of Parietaria judaica pollen, Par j I, is a glycopolypeptide with mol. wt about 10,000. It shows a considerable charge heterogeneity which is mostly due to the carbohydrate prosthetic groups, since treatment with trifluoromethanesulfonic acid yielded a deglycosylated protein with

Five Parietaria officinalis pollen extracts were obtained after respective 0.5, 4, 16, 48, 96 h of extraction in 0.0125 M NH4HCO3 pH 8.7 containing 0.05% NaN3 and 5.7 X 10(-4) M phenylmethylsulphonylfluoride. Conductivity, pH, absorption coefficient at 280 and 360 nm and content in protein and

Par o I, a major allergen of Parietaria officinalis, was purified from the pollen extract. The purified allergen was obtained by ultrafiltration, Sephadex gel filtration and DE-52 ion exchange chromatography: the purified preparation yields a single band in polyacrylamide gel isoelectric focusing

We report the identification and separation of two isoallergen components of Par j I, the major allergen from Parietaria judaica pollen. First, electrophoretic conditions for consistently separating both isoforms in an SDS-PAGE system were established, and mol. wt values of 13,000 (isoallergen IA)