USE OF GLYCOSIDASE DIGESTED HUMAN CHORIONIC GONADOTROPIN β-SUBUNIT TO EXPLAIN THE PARTIAL BINDING OF ECTOPIC GLYCOPROTEIN HORMONES TO CON A

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Abstract
Recent studies have demonstrated that ectopic glycoprotein hormones only partially bind Con A. To investigate the basis for these findings, the Con A binding of ectopic hCGβ from DoT cervical carcinoma cells was examined after digestion with various glycosidases. Ectopic hCGβ only partially bound Con A, as was the case after digestion with neuraminidase and β-galactosidase. However, subsequent digestion with N-acetylhexosaminidase increased Con A binding to 96%. It is apparent that Con A binding of ectopic hCG can be inhibited by a residue removed by N-acetylhexosaminidase, probably extra β-N-acetylglucosamine linked to β-mannose on N-linked oligosaccharides. The method used involved the glycosidase digestion of glycoprotein alkylated under denaturing conditions and was first validated with milligram amounts of standard hCGβ.

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