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A novel lectin, with a molecular mass of 18.6 kDa and a unique N-terminal amino acid sequence, was purified from dried fruiting bodies of the mushroom Hygrophorus russula (Fr.) Quél.. The purification procedure encompassed successive ion exchange chromatography on CM-cellulose, DEAE-cellulose, Q-Sepharose, SPSepharose and Mono S. The hemagglutinating activity of the lectin (NHRL) was stable at temperatures below 50°C and in the presence of 6 mM NaOH or 25 mM HCl. The activity was activated by Cu, Al, Fe, and Pb ions, and inhibited by Hg ions. Among the sugars tested, only mannose and fructose inhibited its hemagglutinating activity.

Isolation and Characterization of a Novel Mannose- and Fructose-Binding Lectin from the Edible Wild Mushroom Hygrophorus russula (Fr.) Quél.