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The lectin-binding properties of serum subunit were studied by lectin affinity chromatography. Normal individuals and most patients with pituitary tumours produced subunit which bound specifically to Concanavalin A–Sepharose (Con A). Some patients with pituitary tumours produced both Con A-reactive subunit and subunit which did not bind to Con A. Concanavalin A–Sepharose-binding subunit from all sources bound strongly to Ricinus communis agglutinin–Sepharose after treatment with neuraminidase. Serum subunit from those patients with pituitary tumours, which did not bind to Con A, bound to wheat germ agglutinin–Sepharose, exhibiting both weakly binding and strongly binding forms. Serum subunit from both patients and controls, which did bind to Con A, showed only weak affinity for wheat germ agglutinin–Sepharose. Neither the low affinity nor the high affinity of serum subunit from any source for wheat germ agglutinin–Sepharose was affected by neuraminidase. These findings show that (a) the predominant pattern of glycosylation of serum subunit from normal controls is a Con A-reactive, biantennate complex oligosaccharide and (b) that the structural alteration which results in serum subunit which does not bind to Con A in some patients with pituitary tumours is not an absence of carbohydrate, rather the subunit contains highly branched, either complex or hybrid oligosaccharides.

J. Endocr. (1984) 103, 111–116