Abstract
The major allergens of birch pollen were separated from most of the non-allergenic antigens as well as from non-proteinic water-soluble components by gel filtration on Sephadex G-100. These allergens appeared homogenous as to their molecular weight which was calculated to be about 20,000. They seemed to consist of at least two, heat stable, differently charged but antigenically similar proteins. The major allergen of alder pollen appeared closely related to those of birch pollen. The results bring up the question of the nature of allergenicity. They are consistent with the notion that a stable structure, a certain molecular weight and ability to induce reagin formation are prerequisites for an allergenic molecule.