The role of polyprenol-bound saccharides as intermediates in glycoprotein synthesis in liver.

It has been reported that liver microsomes catalyze the transfer of glucose from uridine diphosphate glucose to dolichol monophosphate so as to produce dolichol monophosphate glucose. Dolichol is a polyprenol containing about 20 isoprene units. The glucosyl residue of dolichol monophosphate glucose is transferred to an endogenous acceptor on further incubation with liver microsomes. The glucosylated endogenous acceptor appears to be an oligosaccharide of about 20 monosaccharide units bound to dolichol through a phosphate or pyrophosphate bridge. In this paper it is reported that liver microsomes catalyze the transfer of the oligosaccharide from the glucosylated endogenous acceptor to an endogenous protein. This transfer reaction requires the presence of bivalent cations, manganese being more effective than magnesium. The presence of deoxycholate is also required. Besides the glycoprotein, several water-soluble products are also formed. Preliminary evidence indicates that they are glucose, iligosaccharides of different size, and possibly oligosaccharides bound to amino acids.