Purification and characterization of an anti-(A+B) specific lectin from the mushroom Hygrophorus hypothejus

A lectin (HHL) was isolated from the fruiting body of the mushroom Hygropho rus hypothejus by a combination of affinity chromatography on stromas of gr oup B erythrocytes embedded in polyacrylamide gel, and DEAE-trisacryl and g el filtration chromatography. Its molecular mass, as determined by gel filt ration, is estimated to be 68000 kDa and its structure is tetrameric with f our identical subunits assembled with non-covalent bonds. HHL agglutinates specifically A and B blood group erythrocytes and in hemagglutination inhib ition assays, exhibits sugar-binding specificity toward lactose, the anomer ic cc form being more effective than the beta form. (C) 1999 Elsevier Scien ce B.V. All rights reserved.