Isolation of a purified allergen from Kentucky blue grass pollen.
An allergenic fraction, designated as C-I-2-6, was isolated from among the allergenic constituents present in the dialysate of the aqueous extract of defatted Kentucky blue grass (KBG) pollen by a combination of gel filtration, ion-exchange chromatography and preparative isoelectrofocusing. This fraction was shown in consist of glycoprotein with a molecular size corresponding to 10,000 daltons and of two compounds with closely related pI values (4.5--4.9); its protein moiety contained all the amino acids except cysteine. As demonstrated by crossed immunoelectrophoresis with a sheep anti-R serum, fraction C-I-2-6 shared the antigenic determinants of 2 of the 15 antigenic components of the nondialysable components, i.e. retentate (R) of the aqueous extract of KBG pollen. Remarkably, in spite of the markedly lower molecular weight than R, fraction C-I-2-6 possessed all the allergenic determinants of R responsible for inducing murine IgE antibodies.
D000485:Allergens / Q000276:immunology / Q000302:isolation & purification*; D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002850:Chromatography, Gel; D003378:Counterimmunoelectrophoresis; D004591:Electrophoresis, Polyacrylamide Gel; D006241:Haptens; D007525:Isoelectric Focusing; D051379:Mice; D008970:Molecular Weight; D011058:Pollen; D011852:Radioallergosorbent Test; D051381:Rats
D000485:Allergens; D006241:Haptens