In vivo N-glycosylation and fate of Asn-X-Ser/Thr tripeptides.
نویسندگان
چکیده
منابع مشابه
Substrate recognition by oligosaccharyltransferase. Studies on glycosylation of modified Asn-X-Thr/Ser tripeptides.
The minimum primary structural requirement for N-glycosylation of proteins is the sequence -Asn-X-Thr/Ser-. In the present study, NH2-terminal derivatives of Asn-Leu-Thr-NH2 and peptides with asparagine replacements have been tested as substrates or inhibitors of N-glycosylation. The glycosylation of a known acceptor, N alpha-[3H]Ac-Asn-Leu-Thr-NHCH3, was optimized in chicken oviduct microsomes...
متن کاملEnzymatic N-glycosylation of synthetic Asn--X--Thr containing peptides.
The role of polyprenol sugar derivatives in the biosynthesis of certain eukaryotic glycoproteins has been partly described [ 11. Recently lipid pyrophospho-oligosaccharides, postulated as necessary intermediates to initiate N-glycosylation, were shown, when supplied to microsomes, to be effective donors to proteinic acceptors presenting at least one vacant Asn-X-zk sequence: unfolded forms of p...
متن کاملN-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C.
Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons. We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels. The N-glycans of hPC are comple...
متن کاملThe Relationship of Secretion and Activity of Recombinant Factor IX with N-Glycosylation
Background: Human coagulation factor IX (hFIX) is a glycoprotein with two N-glycosylation sites at the activation peptide. Since the activation peptide is removed in mature hFIX, the exact role of N-glycosylation is unclear. To investigate the role of N-glycosylation in the secretion and activity of hFIX, we inhibited N-glycosylation by tunicamycin in the stable Human Embryonic Kidney (HEK)- c...
متن کاملDBU-catalyzed transprotection of N-Fmoc-cysteine di- and tripeptides into S-Fm-cysteine di- and tripeptides.
The transprotection of N-Fmoc-cysteine containing di- and tripeptides possessing a free SH group to produce the corresponding S-Fm-cysteine di- and tripeptides bearing a free amino group is accomplished efficiently with DBU in dry THF. The N-Fmoc to S-Fm transformation mechanism is discussed. S-Fm-Cysteine di- and tripeptides readily form amide bonds on coupling with N-(Pg-α-aminoacyl)benzotria...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)77399-7