Hq. Mo et Ij. Goldstein, ISOLATION AND CHARACTERIZATION OF A FORSSMAN ANTIGEN-BINDING LECTIN FROM VELVET BEAN (MUCUNA-DERRINGIANA) SEEDS, Glycoconjugate journal, 11(5), 1994, pp. 424-431
A Forssman antigen (GalNAc alpha 1-3GalNAc beta 1-3Gal alpha 1-4Gal be
ta 1-4Glc beta 1-1Cer)-binding lectin has been purified from velvet be
an (Mucuna derringiana) seeds by a combination of affinity chromatogra
phy and reversed phase HPLC. This lectin agglutinates both native and
trypsin-treated sheep erythrocytes as well as trypsinized rabbit eryth
rocytes, but neither native rabbit nor human erythrocytes, irrespectiv
e of blood group type. SDS-PAGE and gel filtration chromatography reve
al the lectin to be a homodimer consisting of two 54 kDa subunits link
ed by non-covalent bonds. The results obtained by quantitative precipi
tation, haemagglutination inhibition and TLC overlay assays indicate t
hat the Mucuna lectin specifically recognizes Forssman antigen and For
ssman disaccharide (GalNAc alpha 1-3GalNAc)-related structures.