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

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.) Quel.. The purification procedure encompassed successive ion exchange chromatography on CM-cellulose, DEAE-cellulose, Q-Sepharose, SP-Sepharose and Mono S. The hemagglutinating activity of the lectin (NHRL) was stable at temperatures below 50 degrees C and in the presence of 6 mM NaOH or 25 mM HCl. The activity was activated by Cu2+, Al3+, Fe3+, and Pb2+ ions, and inhibited by Hg2+ ions. Among the sugars tested, only mannose and fructose inhibited its hemagglutinating activity.