J. Verma et al., PURIFICATION AND CHARACTERIZATION OF FUS SI(3596)ASTERISK A 65 KD ALLERGEN OF FUSARIUM-SOLANI, Molecular and cellular biochemistry, 131(2), 1994, pp. 157-166
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.