A basic lectin from bulbs of Arisaema ringens
2008
Yagi, F.(Kagoshima Univ. (Japan)) | Yamashita Higuchi, C. | Minami, Y.
A lectin was purified from bulbs of Arisaema ringens Schoot, using DEAE-Cellulofine column chromatography and chromatofocusing. The purified lectin had the specific activity of 86,000 titer/mg protein/ml and its yield was 1.8%. The homogeneity of the lectin was confirmed by SDS-PAGE. Its isoelectric point was 8.2 and the molecular mass was 12.4kDa. It was only active toward trypsinized rabbit erythrocytes. It was deduced from the hemagglutination inhibition that the lectin recognized mannooligosaccharides and terminal N-acetyllactosamine.
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