Primary structural requirements for N -glycosylation of peptides in rat liver
نویسندگان
چکیده
منابع مشابه
Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes.
Conformational aspects of N-glycosylation have been investigated with a series of proline-containing peptides as molecular probes. The results demonstrate that, depending on the position of the imino acid in the peptide chain, dramatic alterations of glycosylation rates are produced, pointing to a critical contribution of the amino acids framing the 'marker sequence' triplet Asn-Xaa-Thr(Ser) on...
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Neural development requires N-glycosylation regulation of intercellular signaling, but the requirements in synaptogenesis have not been well tested. All complex and hybrid N-glycosylation requires MGAT1 (UDP-GlcNAc:α-3-D-mannoside-β1,2-N-acetylglucosaminyl-transferase I) function, and Mgat1 nulls are the most compromised N-glycosylation condition that survive long enough to permit synaptogenesi...
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Site selectivity of protein N-linked glycosylation is dependent on many factors, including accessibility of the modification site, amino acids that make up the glycosylation consensus sequence and cellular localization of target proteins. Previous studies have shown that the bacterial oligosaccharyltransferase, PglB, of Campylobacter jejuni favors acceptor proteins with consensus sequences (D/E...
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چکیده ندارد.
15 صفحه اولRole of N-glycosylation for the plasma clearance of rat liver secretory glycoproteins.
The clearance of total rat liver secretory glycoproteins and of alpha 1-acid glycoprotein carrying no or different types of oligosaccharide side chains was studied in vivo and in the isolated perfused rat liver. In order to obtain unglycosylated or differently glycosylated forms of secreted glycoproteins, rat hepatocyte primary cultures were incubated with various inhibitors of N-glycosylation....
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1979
ISSN: 0014-5793
DOI: 10.1016/0014-5793(79)80559-1