Isolation and characterization of a 22 kDa protein with antifungal properties from maize seeds

Abstract

We have purified a 22 kDa protein from maize seeds to homogeneity by ammonium sulfate precipitation, chitin extraction and Mono-S column chromatography. The purified protein inhibited the growth of the agronomically important pathogens of potato wilt (Fusarium oxysporum) and tomato early blight (Alternaria solani). Sequence analysis of the purified protein showed that it has 52% homology with the sweet protein thaumatin (Edens, L., Hselinga, L., Klok, R., Ledeboer, A. M., Maat, J., Toonen, M. Y., Visser, C., and Verrips, C. (1982) Gene 18, 1-12), 57% homology with the pathogenesis-related protein (Cornelissen, B. J. C., Huijsduijnen, R. A. M., and Bol, J. F. (1986) Nature 321, 531-532) and 99% homology with the 22 kDa trypsin/alpha-amylase inhibitor (Richardson, M., Valdes-Rodriguez, S., and Blanco-Labra, A. (1987) Nature 327, 432-434).