Purification and characterization of a lectin from the mushroom Hypsizigus marmoreus

•A novel lectin, HML, was purified from the edible mushroom Hypsizigus marmoreus by repeated chromatography.•The molecular weight and partial amino acid sequence of HML were determined.•The result of the hemagglutination inhibition test suggested that HML belongs to the group with specificity towards N-glycans.

HML (Hypsizigus marmoreus lectin) was isolated from the mushroom Hypsizigus marmoreus using CM cation exchange, bovine submaxillary gland mucin affinity column and TSK-GEL G3000SW gel filtration chromatography. The results of SDS-PAGE, MALDI-TOF MS and gel filtration analysis of HML indicated that the lectin was a dimer with each subunit of 9.5 kDa. The partial amino acid sequences of HML were determined by N-terminal sequencing of peptides obtained by trypsin or Glu-C endopeptidase digest of the lectin. In the hemagglutination inhibition assay, HML did not bind to any mono- or oligo-saccharides tested. Among the glycoproteins examined, asialo-fetuin was the strongest inhibitor.