Cell-surface, Lectin-reactive Glycoproteins

Cell-surface, Lectin-reactive Glycoproteins 

The investigation of lectin-cell interaction by means of binding studies with labelled lectins is informative, but limited, in that the carbohydrate-binding sites of most lectins are still incompletely characterized. A comprehensive understanding of lectin-cell interaction requires, in addition to pure lectins of known properties, highly purified, lectin-reactive molecules that are also well characterized. In very few (if, indeed, any) cases has this ideal been achieved. It is to be hoped that such more-complete analyses will be forthcoming. 

Lectin-reactive glycoproteins of the erythrocyte membrane have been studied extensively. Of these, the major sialoglycoprotein has 

Pospisilova and coworkers185 investigated the chemical structure of the pea lectin-reactive glycopeptide isolated by Kubanek and coworkers.844 After refining the chemical analysis, and applying glycosidase digestion, they proposed the structure depicted in formula 16. Despite 

Human-platelet membranes have been extracted with lithium 3,5-diiodosalicylate, and the soluble glycoproteins separated on O-phosphonocellulose.849 The purified, membrane glycoprotein, molecular weight 100,000, was immunochemically identical to a sample purified from platelet-membrane extract by means of con A-Sepharose affinity chromatography. No further characterization was reported, 

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VIII. Cell-surface, Lectin-reactive Glycoproteins. 317... 

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