期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1977
卷号：74
期号：1
页码：134-138
DOI：10.1073/pnas.74.1.134
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
