Abstract
An N-acetylglucosamine-binding lectin with a molecular mass of 32 kDa was isolated from fresh sclerotia of the edible mushroom Pleurotus tuber-regium. Its N-terminal sequence exhibited some similarity to that of Agaricus bisporus lectin. The isolation procedure was simple, involving (NH 4) 2SO 4 precipitation, ion exchange chromatography on DEAE–cellulose, affinity chromatography on N-acetyl- d-glucosamine–agarose, and gel filtration by fast protein liquid chromatography on Superdex 75. The lectin exhibited hemagglutinating activity toward trypsinized rabbit erythrocytes but not toward untrypsinized rabbit erythrocytes.
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