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 Hygrophorus hypothejus by a combination of affinity chromatography on stromas of group B erythrocytes embedded in polyacrylamide gel, and DEAE-trisacryl and gel filtration chromatography. Its molecular mass, as determined by gel filtration, is estimated to be 68000 kDa and its structure is tetrameric with four identical subunits assembled with non-covalent bonds. HHL agglutinates specifically A and B blood group erythrocytes and in hemagglutination inhibition assays, exhibits sugar-binding specificity toward lactose, the anomeric alpha form being more effective than the beta form.

Expression of Tn antigen and N-acetyllactosamine residues in malignant and benign human breast tumors detected by lectins and monoclonal antibody 83D4.

Expressions of the carcinoembryonic Tn antigen studied with VVA-B4 and GSI-A4 lectins with the monoclonal antibody 83D4 and of N-acetyllactosamine residues with ECA and LSL lectins, were examined in 54 malignant or benign human breast tumors. Positive membrane labelling with lectins and 83D4 MAb occured in benign cases indicating that modification of glycoconjugates may precede the cytologic anomalies. In fibroadenoma, fibrocystic dystrophy, ductal hyperplasia and grade I invasive ductal carcinomas, the binding sites for all lectins and 83D4 MAb were essentially on the cell membrane with labelling of both apical and basolateral compartments.

Characterization of a Lectin from Lactarius deterrimus (Research on the Possible Involvement of the Fungal Lectin in Recognition between Mushroom and Spruce during the Early Stages of Mycorrhizae Formation).

A lectin (LDetL) was isolated from carpophores of the mushroom Lactarius deterrimus, a specific symbiont of the spruce, by a combination of affinity, hydroxylapatite, and gel-filtration chromatography. Its molecular mass, as determined by gel filtration, is about 37,000 D, and its structure is dimeric, with two identical subunits assembled by noncovalent bonds. It appeared homogeneous on high-performance liquid chromatography gel filtration, but isoelectric focusing revealed microheterogeneity, with a main band in the pH zone near 6.

Isolation and characterization of a lectin from the mushroom, Lactarius deliciosus.

A lectin (LDL) has been isolated from carpophores of the edible mushroom, Lactarius deliciosus, using a combination of affinity chromatography on stromas of group O erythrocytes embedded in polyacrylamide gel and hydroxylapatite, and gel filtration chromatography. Its molecular weight, as determined by gel filtration, is about 37,000 and its structure is dimeric, with two distinct types of subunits (about 19,000 and 18,000). It appeared homogeneous on HPLC gel filtration, but exhibited microheterogeneity on isoelectric focusing.