Abstract
The changes in the circular dichroism of concanavalin A, peanut agglutinin and the pea lectin produced by the binding of simple glycosides and complex glycopeptides from immunoglobulins, fetuin and ovalbumin are reported. Three oligosaccharides of mannose behaved identically with concanavalin A, and three galactosides behaved identically with peanut agglutinin. In contrast, the glycopeptides which have higher K a values generally produced much smaller changes in circular dichroism than the simple glycosides, suggesting the binding sites on lectins are preformed to some extent for more complex saccharides.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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