Isolation and characterization of a mannose-binding lectin from leaves of the Chinese daffodil Narcissus tazetta.
A mannose-binding lectin was isolated from leaves of the Chinese daffodil Narcissus tazetta (family Amaryllidaceae) using a procedure that comprised extraction with aqueous buffer, ammonium sulfate precipitation, ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel Blue gel and mannose-agarose, and FPLC-gel filtration on Superose 12. The lectin was adsorbed on mannose-agarose and unadsorbed on DEAE-cellulose and Affi-gel Blue gel. It was an unglycosylated homodimer with a molecular mass of 26 kDa. Analysis of the N-terminal sequence of the N. tazetta lectin revealed considerable homology to lectins from the daffodil Narcissus pseudonarcissus, the snowdrop Galanthus nivalis (family Amaryllidaceae), the tulip Tulipa, and Kidachi aloe Aloe arborescens (family Liliaceae), and the orchid lectins (family Orchidaceae). The most striking likeness exists among the Amaryllidaceae lectins. The N. tazetta lectin exhibits hemagglutinating activity toward rabbit erythrocytes.
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Department of Biochemistry, Chinese University of Hong Kong, Shatin, New Territories, China. vincent-ooi@cuhk.edu.hk
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D050260:Carbohydrate Metabolism; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D027801:Galanthus; D006384:Hemagglutination; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification*; D008358:Mannose / Q000378:metabolism*; D037121:Plant Lectins; D010940:Plant Proteins / Q000378:metabolism*; D013997:Time Factors
D037102:Lectins; D037121:Plant Lectins; D010940:Plant Proteins; D008358:Mannose