[Purification of lectin from Paris quadrifolia L. and comparison of its carbohydrate-binding specificity with other lectins of the Liliaceae family].
Lectin from rhizomes of Paris quadrifolia I. was purified by affinity chromatography on cross-linked ovomucine with yield of 75 mg per 1 kg of fresh rhizomes. Purified lectin gave a single band on gel disk electrophoresis at pH 4.5 and two bands at pH 8.9. Electrophoresis in gradient 15-20% polyacrylamide gel in the presence of DS-Na at pH 8.9 has revealed two distinct bands with Mm 12.8 and 11.5 kDa. Gel chromatography on Sephadex G-200 has discovered two proteins with Mm 50 and 102 kDa. The agglutinating activity is inhibited by N-acetylneuraminic acid and several sialyl-glycoproteins. Lectins with such specificity were also discovered in grasses Scilla bifolia I, Gagea lutea I. and Polygonatum multiflorum (L) All.
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D050260:Carbohydrate Metabolism; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000378:metabolism; D037102:Lectins / Q000302:isolation & purification*; D037121:Plant Lectins; D018517:Plant Roots / Q000378:metabolism; D010944:Plants / Q000378:metabolism*; D011485:Protein Binding
D006023:Glycoproteins; D037102:Lectins; D037121:Plant Lectins