De novo synthesis and glycosylation of the MOPC-46B mouse immunoglobulin light chain in cell-free extracts

Abstract

The mRNA for the mouse MOPC-46B K chain, a glycorportein, was prepared translated in Ehrlich ascites cell-free extract. A polypeptide product similar to the MOPC-46B kappa chain was identified by its antigenic properties and by analysis of the products of tryptic digestion. In addition, the cell-free product was glycosylated after translation. It appeared that glycosylation of the cell-free product occurred on the same tryptic peptide glycosylated by intact cells. The characteristics and requirements of glycosylation are described. The presence of Mn2+ was a major requirement.