Oligosaccharide moieties of glycoprotein hormones: bovine lutropin resists enzymatic deglycosylation because of terminal O-sulfated N-acetylhexosamines.

The oligosaccharides of the bovine pituitary gonadotropin lutropin are N-linked to asparagine residues. These carbohydrates are unusual in that, although they contain the mannose, N-acetylglucosamine, and fucose typical of N-linked oligosaccharides, they also contain one residue of N-acetylgalactosamine but insignificant amounts of sialic acid or galactose. These oligosaccharides exhibit complete resistance to several exoglycosidases. This is in contrast to the ready release of peripheral sugars from human chorionic gonadotropin, a placenta hormone which has oligosaccharides of the complex type with terminal sialic acid and galactose residues. Stability of the lutropin hexosamines to periodate oxidation and reduction (Smith degradation) together with other data show that one residue of N-acetylgalactosamine and one of N-acetylglucosamine are peripheral to two periodate-sensitive mannose residues. The insensitivity to periodate of these two terminal amino sugars is found to result from a sulfate group covalently linked to each; sulfation of these hexosamines is also the most probable reason for the resistance to enzymatic deglycosylation. The alpha subunits of bovine thyrotropin and human pituitary lutropin also contain sulfate, in contrast to human chorionic gonadotropin. The results indicate that sulfating enzymes are present in the pituitary and that sulfation of peripheral sialic acids in the placental gonadotropin. The data lead to a partial structure for the oligosaccharides of bovine LH as follows: (formula see text).