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Maackia amurensis lectin II (MAH) is the hemagglutinin isolectin from Maakia seeds. It is a glycoprotein consisting of four subunits. The molecular weight of the lectin is about 140,000 resolvable by SDS gel electrophoresis into two bands of 34,000 and 36,000 daltons. The isoelectric point of this lectin is about pH 4.7 but demonstrates some charge heterogeneity.
Although the specificity of this lectin is not well defined, MAL II appears to bind only particular carbohydrate structures that contain sialic acid. Unlike SNA which seems to prefer structures with (a-2,6) linked sialic acid, MAL II appears to bind sialic acid in an (a-2,3) linkage. While fetuin is a poor inhibitor, glycophorin is a very potent inhibitor of MAL II binding. Tissue staining patterns are also very different among MAL I, SNA and MAL II. |