Enzymatic conversion of proteins to glycoproteins.

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Abstract
The enzymatic transfer of the oligosaccharide moiety from an oligosaccharide-lipid to denatured forms of 3 secretory proteins: ovalbumin, .alpha.-lactalbumin and RNase A was demonstrated utilizing a membrane fraction from hen oviduct. Based on a survey of 10 proteins denatured by sulfitolysis, the presence of the tripeptide sequence .**GRAPHIC**. (X represents a variable amino acid) appears to be necessary but not sufficient for the protein to serve as acceptor in vitro. Unfolding of the polypeptide chain may be required in order to expose sited for carbohydrate attachment.