| Literature DB >> 264667 |
Abstract
The enzymatic transfer of the oligosaccharide moiety from an oligosaccharide-lipid to denatured forms of three secretory proteins--ovalbumin, alpha-lactalbumin, and ribonuclease A--has been demonstrated utilizing a membrane fraction from hen oviduct. Based on a survey of 10 proteins denatured by sulfitolysis, the presence of the tripeptide sequence -Asn-X-Thr-Ser- (X represents a variable amino acid) appears to be necessary but not sufficient for the protein to serve as acceptor in vitro. The results of this investigation also suggest that unfolding of the polypeptide chain is required in order to expose sites for carbohydrate attachment.Entities:
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Year: 1977 PMID: 264667 PMCID: PMC393212 DOI: 10.1073/pnas.74.1.134
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205