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KMID : 0578319970070020214
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Molecules and Cells
1997 Volume.7 No. 2 p.214 ~ p.219
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Purification and characterization of an Antifungal Re-5 Protein from Pumpkin Leaves
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cheong, Na Eun
Choi, Yeon Ok/Kim, woe yeon/Bae, In Suck/Cho, Moo Je/hwang, Inwhan/Kim, Jae Won
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Abstract
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A 28-kDa antifungal PR-5 protein (PLTP) was purified from pumpkin leaves to homogeneity by using ammonium sulfate fractionation, a regenerated chitin column, and reversed-phase column chromatographies on butyl-Toyopearl and HPLC C_(18) columns. Analysis of 14N-terminal amino acid sequences of PLTP shows 100% sequence identity to those of two PR-5 proteins, NP24 from tomatoes and AP24 from tobacco. The identical sequence also exhibited high amino acid sequence homology to that of an osmtin-like protein (OLP;71%) from tobacco cells and thaumatin (64%), a sweet-tasting protein of Thaumatococcus danielli Bench. When the PLTP was immuno-blotted with antiserum raised against the tobacco OLP, the OLP antibody specifically cross-reacted with the PLTP, suggesting that they share several common epitopes in their tertiary structure of the proteins. The purified PLTP rapidly lyzed hyphal tips of Neurospora crassa at a concentration greater than 200nM and significantly inhibited the fungal growth of Fusarium oxysporum in an agar-disc plate at a concentration greater than 2μM. It also showe a synergistic effect with nikkomycin, a chitin synthase inhibitor, for the growth inhibition of Candida albicans.
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