Purification and properties of a lectin from ascomycete mushroom, Ciborinia camelliae.

Abstract A lectin was isolated from an ascomycete mushroom, Ciborinia camelliae which was specific to N -acetyl- d -galactosamine. On SDS-polyacrylamide gel electrophoresis; this lectin gave a single band of ∼17-kDa in the presence of 2-mercaptoethanol, but formed dimers, trimers and tetramers in its absence. Amino acid analysis revealed the lectin contained two cysteines and no methionine. The N-terminal sequence was determined up to residue 21, and no homologous proteins including other ascomycete lectins were found.