[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.