An antifungal protein named PaAFP was isolated and purified from the seeds of Pachyrrhizus erosus by extraction with PB buffer, S Sepharose Fast Flow, CM 52 cellulose and Sephadex G 75 column chromatography. On potato sucrose agar medium, the purified protein obviously inhibited the growth of the important edible fungus pathogens Trichoderma viride and Chrysosporium luteum at 6 2 μg and 12 5 μg per disc respectively. The molecular weight was about 14 kD by SDS PAGE and HPLC. The isoelectric point was pH7 5. Analysis of the composition of amino acids showed that this protein was rich in Asx, but lacking in Met.
