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Cell-surface, Lectin-reactive Glycoproteins

Cell-surface, Lectin-reactive Glycoproteins [Pg.317]

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. [Pg.318]

Lectin-reactive glycoproteins of the erythrocyte membrane have been studied extensively. Of these, the major sialoglycoprotein has [Pg.318]

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 [Pg.321]

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, [Pg.325]


VIII. Cell-surface, Lectin-reactive Glycoproteins. 317... [Pg.128]


See other pages where Cell-surface, Lectin-reactive Glycoproteins is mentioned: [Pg.61]    [Pg.141]    [Pg.150]    [Pg.318]    [Pg.368]    [Pg.53]   


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Cell surface

Cell surface glycoprotein

Glycoproteins lectins

Reactive surface

Surface glycoproteins

Surface reactivity

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