Isolation and characterization of a Forssman antigen-binding lectin from velvet bean (Mucuna derringiana) seeds.
A Forssman antigen (GalNAc alpha 1-3GalNAc beta 1-3Gal alpha 1-4Gal beta 1-4Glc beta 1-1Cer)-binding lectin has been purified from velvet bean (Mucuna derringiana) seeds by a combination of affinity chromatography and reversed phase HPLC. This lectin agglutinates both native and trypsin-treated sheep erythrocytes as well as trypsinized rabbit erythrocytes, but neither native rabbit nor human erythrocytes, irrespective of blood group type. SDS-PAGE and gel filtration chromatography reveal the lectin to be a homodimer consisting of two 54 kDa subunits linked by non-covalent bonds. The results obtained by quantitative precipitation, haemagglutination inhibition and TLC overlay assays indicate that the Mucuna lectin specifically recognizes Forssman antigen and Forssman disaccharide (GalNAc alpha 1-3GalNAc)-related structures.
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Department of Biological Chemistry, University of Michigan, Ann Arbor 48109.
Goldstein
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D000595:Amino Acid Sequence; D000818:Animals; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity; D002855:Chromatography, Thin Layer; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000737:chemistry*; D005577:Forssman Antigen / Q000378:metabolism*; D006386:Hemagglutination Tests; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D037121:Plant Lectins; D010946:Plants, Medicinal; D011817:Rabbits; D017386:Sequence Homology, Amino Acid; D012756:Sheep
D037102:Lectins; C092857:Mucuna derringiana lectin; D037121:Plant Lectins; D005577:Forssman Antigen