The cell-free biosynthesis of the glycoprotein of membranes from Ehrlich ascites carcinoma cells.

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Abstract
The incorporation of glucosamine and galactose into soluble and membrane glycoproteins is described. The enzymes which incorporate glucosamine and galactose (from UDP[uridine diphosphate]-galactose) into TCA[trichloroacetic acid]-insoluble glycoproteins were found to reside in a postmicrosomal particulate fraction. It was postulated that the oligosaccharides, synthesized by this fraction, are attached to a protein receptor at the membranes bearing microsomes as a step in the eventual buildup of the surface membrane. The incorporation of monosaccharides was stimulated by ATP[adenosine triphosphate] and other monosaccharides, but not by UTP[uridine triphosphate], GTP[guanosine triphosphate], CTR [cytidine triphosphate], RNase[adenosine triphosphate], and puromycin. The incorporation of monosaccharides was contrasted with the incorporation of amino acids into soluble and membrane fractions.