核糖体 - UDP - N - 乙酰半乳糖胺复合物在体外蛋白质糖基化起始过程中的参与。
The participation of ribosome-UDP-GalNAc complex in the initiation of protein glycosylation in vitro.
作者信息
Paszkiewicz-Gadek A, Porowska H, Gindzieński A
机构信息
Department of General and Organic Chemistry, Institute of Chemistry Medical Academy, Białystok, Poland.
出版信息
Acta Biochim Pol. 2000;47(2):421-6.
The gastric epithelial cells ribosome-UDP-GalNAc complex is a donor of UDP-GalNAc as the substrate for N-acetylgalactosaminyltransferase, which catalyse the transfer of GalNAc residue to the polypeptide, existing on polysomes. It was observed that the deglycosylated porcine mucin and synthetic peptide (PTSSPIST) can be also glycosylated with participation of N-acetylgalactosaminyltransferase and ribosome-UDP-GalNAc complex. The probability of the ribosome-UDP-GalNAc complex as an intermediate in the O-glycosylation is considered.
胃上皮细胞核糖体 - UDP - N - 乙酰半乳糖胺复合物是作为N - 乙酰半乳糖胺基转移酶底物的UDP - N - 乙酰半乳糖胺的供体，该酶催化将N - 乙酰半乳糖胺残基转移至存在于多核糖体上的多肽。据观察，去糖基化的猪粘蛋白和合成肽（PTSSPIST）在N - 乙酰半乳糖胺基转移酶和核糖体 - UDP - N - 乙酰半乳糖胺复合物参与下也能被糖基化。核糖体 - UDP - N - 乙酰半乳糖胺复合物作为O - 糖基化中间体的可能性得到了考虑。
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