Abstract
The allergen extract of Phleum pratense pollen was fractionated by gel filtration on a Sephadex G-75 column. The allergenically active fraction was concentrated and purified further by ion-excange chromatography on a hydroxyapatite column. The purified allergen preparation contained proteins with molecular weights between 10,000 and 40,000 daltons and contained no free carbohydrate. The purified extract was significantly more allergenically active than the whole extract, as judged from the results. of RAST inhibition assay.
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