Evidence for a single glycan moiety in rabbit serum transferrin and location of the glycan within the polypeptide chain.
نویسندگان
چکیده
The sequential removal of N-acetylneuraminic acid from rabbit serum transferrin has been followed by urea-polyacrylamide gel electrophoresis. The electrophoretic pattern is consistent with the presence of a single biantennary glycan chain. From the amino acid sequence of the carbohydrate-containing cyanogen bromide fragment we have shown that the glycan is attached to an asparaginyl side chain at a position equivalent to residue 491 in the sequence of human serum transferrin.
منابع مشابه
Bi-and tri-antennary human transferrin glycopeptides and their affinities for the hepatic lectin specific for asialo-glycoproteins.
Glycopeptides were isolated from a proteolytic digest of human transferrin. After mild acid hydrolysis the desialylated glycopeptides were labelled by the galactose oxidase/NaB(3)H(4) procedure and then fractionated by Sephadex-gel filtration or by anion-exchange chromatography. Either technique allowed separation of the two heterosaccharide chains (designated glycan I and glycan II) previously...
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that concanavalin A recognizes the G l c N A c ( ~ l 2 ~ M a n ( a 1 3 or -6) residues of the transferrin glycan (see above). Moreover, the bird structure is the most suitable from the glycan biosynthesis point of view because all the glycosylable hydroxyl groups are perfectly accessible to glycosyltransferases, as shown in Fig. l(a): substitution in the C-4 position of the /kmannose(3) by an a...
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Accompany with quantitative changes in concentration of acute protein there are qualitative alterations in the carbohydrate moiety (glycosylation) of these proteins in different disease. Haptoglobin (Hp) is one of the human acute phase proteins that undergoes glycosylation changes in disease. There is evidence that glycosylation of Hp changes in ovarian cancer, rheumatoid arthritis and liver ...
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ورودعنوان ژورنال:
- FEBS letters
دوره 238 1 شماره
صفحات -
تاریخ انتشار 1988