Hexiang Wang

Dendrocin, a distinctive antifungal protein from bamboo shoots

An antifungal protein, with a molecular weight of 20 kDa and an inhibitory action on mycelial growth in the fungi Fusarium oxysporum, Botrytis cincerea, and Mycosphaerella arachidicola, was isolated from fresh bamboo shoots. The protein, designated dendrocin, was unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel and CM-Sepharose. Dendrocin showed only limited similarity in N-terminal sequence to thaumatin-like proteins, unlike other thaumatin-like proteins which closely resemble each other. Its molecular weight was also lower than those of the previously reported thaumatin-like proteins. The protein was devoid of hemagglutinating and ribonuclease activities found in some antifungal proteins.

A novel lectin from the wild mushroom Polyporus adusta.

A lectin with antiproliferative activity toward tumor cell lines and mitogenic activity toward splenocytes was isolated from the mushroom Polyporus adusta. The lectin was composed of two identical subunits each with a molecular weight of 12 kDa. It was adsorbed on both DEAE-cellulose and Q-Sepharose and unadsorbed on CM-Sepharose. The hemagglutinating activity of the lectin was inhibited by turanose and by a large variety of other carbohydrates. It was adversely affected in the presence of NaOH or HCl at a concentration of 7.5mM and above, and when the ambient temperature was raised above 70 degrees C. All divalent and trivalent metallic chlorides tested at 1.25-10mM including CaCl(2), MgCl(2), ZnCl(2), MnCl(2), and AlCl(3), did not alter the hemagglutinating activity of the lectin. FeCl(3) at 10mM caused the hemagglutinating activity to increase by 100%, but it did not change the lectin activity when tested at lower concentrations up to 5mM.