The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex-type Asn-linked oligosaccharides containing terminal sialic acid-linked alpha-2,3 to penultimate galactose residues.
作者： W C Wang , R D Cummings
DOI: 10.1016/S0021-9258(18)68821-0
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摘要: We recently reported that the purified leukoagglutinin (designated MAL) from seeds of leguminous plant Maackia amurensis is a potent for mouse lymphoma cell line BW5147 (Wang, W.-C., and Cummings, R. D. (1987) Anal. Biochem. 161,80). others have shown this lectin weak hemagglutinin human erythrocytes (Kawaguchi, T., Matsumoto, I., Osawa, T. (1974) J. Biol. Chem. 249, 2786). now report leukoagglutination by MAL inhibited low concentrations 2,3-sialyllactose (NeuAc alpha 2,3Gal beta 1,4Glc), but it not either 2,6-sialyllactose 2,6Gal beta-1,4Glc), lactose, or free NeuAc. To further study carbohydrate-binding specificity lectin, we investigated interactions immobilized with glycopeptides prepared glycoproteins. found interacts high affinity complex-type tri- tetraantennary Asn-linked oligosaccharides containing outer sialic acid residues linked 2,3 to penultimate galactose residues. Glycopeptides only 2,6 did interact detectably lectin. Our analyses indicate chains are dependent on linkages branching pattern mannose presence poly-N-acetyllactosamine sequences.
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