Studies with purified house dust allergen and observations on the nature of its polypeptide constituent

Abstract

Purified house dust allergen has been subjected to several analytical procedures. Electrophoretic and ultracentrifugal studies showed the allergen to be a mixture of closely related skin-reactive mucoproteins. Dinitrophenylation of the allergen indicated the carbohydrate moiety to be connected to the polypeptide by N-glycosidic linkages. Only a few of the molecules probably have a free (alanine)-α-amino end group. Amino acids are readily released from the carboxyl end of the peptide chain by treatment with alkali. The allergen is resistant to the action of trypsin and chymotrypsin, but is destroyed by incubation with pepsin.

The significance of these findings is discussed.