Variation in the core and branch carbohydrate sequences of serum glycoprotein hormone alpha subunit as determined by lectin affinity chromatography.

Serum alpha subunits from patients with pituitary tumours and from normal controls were studied for their ability to bind to Lens culinaris agglutinin-Sepharose (LCA), L-phytohaemagglutinin-agarose (L-PHA) and soybean agglutinin-Sepharose (SBA). Serum alpha subunits from normal controls which had previously been shown to bind to Concanavalin A-Sepharose (Con A) were not retained by LCA. In contrast, Con A-reactive alpha subunits from patients with pituitary tumours bound specifically to LCA. Non-Con A-reactive alpha subunits from patients with pituitary tumours were also largely not bound to LCA, but were retained by L-PHA. No alpha subunits from any source bound to SBA. These results indicate that the structural alterations resulting in non-Con A-reactive serum alpha subunits include highly branched complex oligosaccharides in addition to the hybrid-type glycans previously described. The increased branching appears to be associated with fucosylation in the core region of the oligosaccharides. Serum alpha subunit from any source appears to be devoid of terminal N-acetylgalactosamine residues. These structural modifications may be related to the variable biological activity of alpha subunit which has been reported.