Pless D D, Lennarz W J
Proc Natl Acad Sci U S A. 1977 Jan;74(1):134-8. doi: 10.1073/pnas.74.1.134.
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.
利用母鸡输卵管的膜部分,已证明寡糖部分可从寡糖脂酶促转移至三种分泌蛋白(卵清蛋白、α-乳白蛋白和核糖核酸酶A)的变性形式。基于对10种经亚硫酸氢盐裂解变性的蛋白质的研究,三肽序列-Asn-X-Thr-Ser-(X代表可变氨基酸)的存在似乎是蛋白质在体外作为受体的必要条件,但并不充分。该研究结果还表明,多肽链的展开是暴露碳水化合物附着位点所必需的。