PURIFICATION AND CHARACTERIZATION OF FUS SI(3596)ASTERISK A 65 KD ALLERGEN OF FUSARIUM-SOLANI

A component of Fusarium solani (F. solani), identified as the major al lergen, Fus s I-3596 was purified to homogeneity from culture filtrat e (CF) by means of anion-exchange column chromatography, gel filtratio n and FPLC. The homogeneity of Fus s I-3596 was assessed by IEF, PAGE , SDS-PAGE (non-reducing), immunoblot and HPLC. Fus s I-3596 was isol ated as a glycoprotein of MW 65 kd and pI 3.6. The IgE ELISA-inhibitio n assay after periodate treatment of the fraction showed a lower IgE b inding capacity suggesting involvement of carbohydrate moiety in IgE b inding reactions of the allergen. Peptide fragments of Fus s I-3596 o btained after CNBr and trypsin treatment were analysed by immunoblotti ng for their allergenicity. This study indicated that there could be a t least 3 allergenic determinants in the major allergen, Fus s I-3596 of F. solani CF.