Toxin protein from Ustilago maydis virus SH14 isolated in Korea was purified using ethanol precipitation, cation exchange, gel filtration and anion exchange chromatography. The molecular weight of the purified protein was estimated to be 8.3 kDa by SDS-PAGE analysis. The Nterminal sequence of the protein is L-G-I-N-C(K)-R-G-S-S-Q--C(K)-G-L-S-G which is highly homologous with that of P4 toxin, but the amino acid composition and electrophoretic mobility in a native PAGE of the toxin protein were totally different from those of P4 toxin respectively. The SH14 toxin was shown to have immunological cross-reactivity about 50% with P4 toxin when examined by Western hybridization.