| Higher eukaryotic organisms glycosylate proteins in a species-specific and organ-specific manner. The oligosaccharide moieties of glycoproteins have been shown to effect the structure and function of the proteins in many cases. Recombinant proteins have been expressed in bacterial and mammalian cell lines, producing proteins that are either nonglycosylated, or glycosylated in a typical mammalian manner. With the use of lower eukaryotic cell lines, particularly yeast and insect cells, it is important to determine the glycosylation capabilities of these cells.; The results presented here elucidate the glycosylation of recombinant proteins expressed in the yeast Pichia pastoris, and the Drosophila S2 cell line. The recombinant proteins expressed are involved in the human circulatory system. It was determined that both cell lines are capable of producing both N-linked and O-linked type oligosaccharides. P. pastoris-expressed proteins contained glycans which were typical of other yeasts, but somewhat smaller. The Drosophila-expressed proteins contained glycans that were typical of other insect cell lines. |
