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J. Biol. Chem., Vol. 263, Issue 10, 4576-4585, 04, 1988
WC Wang and RD Cummings
We recently reported that the purified leukoagglutinin (designated MAL)
from the seeds of the leguminous plant Maackia amurensis is a potent
leukoagglutinin for the mouse lymphoma cell line BW5147 (Wang, W.-C., and
Cummings, R. D. (1987) Anal. Biochem. 161,80). We and others have shown
that this lectin is a weak hemagglutinin of human erythrocytes (Kawaguchi,
T., Matsumoto, I., and Osawa, T. (1974) J. Biol. Chem. 249, 2786). We now
report that leukoagglutination by MAL is inhibited by low concentrations of
2,3-sialyllactose (NeuAc alpha 2,3Gal beta 1,4Glc), but it is not inhibited
by either 2,6-sialyllactose (NeuAc alpha 2,6Gal beta-1,4Glc), lactose, or
free NeuAc. To further study the carbohydrate- binding specificity of this
lectin, we investigated the interactions of immobilized MAL with
glycopeptides prepared from the mouse lymphoma cell line BW5147 and from
purified glycoproteins. We found that immobilized MAL interacts with high
affinity with complex-type tri- and tetraantennary Asn-linked
oligosaccharides containing outer sialic acid residues linked alpha 2,3 to
penultimate galactose residues. Glycopeptides containing sialic acid linked
only alpha 2,6 to penultimate galactose did not interact detectably with
the immobilized lectin. Our analyses indicate that the interactions of
complex-type Asn- linked chains with the lectin are dependent on sialic
acid linkages and are not dependent on either the branching pattern of the
mannose residues or the presence of poly-N-acetyllactosamine sequences.
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
Department of Biochemistry, School of Chemical Sciences, University of Georgia, Athens 30602.
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