Two isolectins from leaves of winged bean, Psophocarpus tetragonolobus (L.) DC.
Two isolectins were isolated from leaves of winged bean and characterized. They differed from each other in terms of their immunological properties, hemagglutinating activities, sugar inhibition patterns, and amino acid compositions. Both lectins were acidic and one of them (L-I), which was inactive toward trypsinized human type O erythrocytes, was similar to one of green shell lectins (WGS-1); which resembled basic seed lectin in its immunological properties. The amino-terminal sequence of L-I was homologous to that of WGS-1. The amino acid composition of L-I was similar to that of basic seed lectin, but the extent of the homology between amino-terminal sequences was low when L-I and basic seed lectin were compared. Examination by ELISA revealed that L-I and WGS-1 were distinct from the basic lectins of seeds and tuberous roots. L-I had a disulfide bridge between two subunits and it exhibited high hemagglutinating activity toward human type A erythrocytes, as compared to its activity toward other erythrocytes. By contrast, the properties of a second acidic lectin from winged bean leaves (L-II) were very similar to those of acidic lectins from seeds and tuberous roots, and the similarities extended as far as the immunological properties.
Yagi
F
F
Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Japan.
Sawada
R
R
Imada
T
T
Toyonaga
S
S
Tadera
K
K
Ishihata
K
K
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D004797:Enzyme-Linked Immunosorbent Assay / Q000379:methods; D007887:Fabaceae / Q000737:chemistry*; D006386:Hemagglutination Tests; D037102:Lectins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D018515:Plant Leaves / Q000737:chemistry*; D037121:Plant Lectins; D010946:Plants, Medicinal; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
D000596:Amino Acids; D037102:Lectins; D037121:Plant Lectins