Abstract
A galactose-specific lectin isolated from Ricinus communis beans has been covalently coupled to Sepharose 4B activated with cyanogen bromide. The immonolized lectin retains its polysaccharide-binding property. The Sepharoselectin can be used for the purification of polysaccharides containing terminal nonreducing galactose. Only a small fraction of “native fetuin’ and ‘native ceruloplasmin’ are retarded on Sepharose-lectin. On analysis it was observed that hey had a lower content of sialic acid as compared to the native and unbound glycoproteins (sialated fractions). However, on desialation, fetuin and ceruloplasmin were completely adsorbed to Sepharose-lectin. The asialoglycoproteins interact strongly with Sepharose-lectin as compared to ‘partially sialated glycoproteins’. This has been attributed to the exposure of galactose residues of these glycoproteins on enzymatic desialation. These experiments demonstrated that Sepharose-lectin interacts with glycoproteins through their terminal, nonreducing galactose. On the basis of these experiments it is suggested that Sepharose-lectin can be used as an analytical tool for separation of ‘fully sialated glycoproteins’ from the ‘partially sialated glycoproteins’.
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