Read e-book online Glycoproteins PDF

By R. Colin Hughes

ISBN-10: 0412241501

ISBN-13: 9780412241505

The scholar of organic technological know-how in his ultimate years as an undergraduate and his first years as a graduate is anticipated to realize a few familiarity with present learn on the frontiers of his self-discipline. New learn paintings is released in a puzzling range of courses and is unavoidably fascinated about the trivialities of the topic. The sheer variety of learn journals and papers additionally motives confusion and problems of assimilation. evaluate articles frequently presuppose a historical past understand­ ledge of the sector and are unavoidably particularly limited in scope. there's hence a necessity for brief yet authoritative introductions to these parts of recent organic learn that are both now not handled in typical introductory textbooks or will not be handled in enough aspect to permit the scholar to move on from them to learn scholarly stories with revenue. This sequence of books is designed to fulfill this desire. The authors were requested to provide a quick define in their topic assuming that their readers could have learn and remembered a lot of a customary introductory textbook of biology. This define then units out to supply through construction in this foundation, the conceptual framework during which glossy study paintings is progressing and goals to offer the reader a sign of the issues, either conceptual and useful, which needs to be conquer if development is to be maintained.

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Thr. Pro. Thr. Pro. Thr. Pro. Thr. Pro. Thr. Pro. Thr. Pro. 0 100 Pro. Pro. Pro. Pro. Pro. Pro. 101 Pro. Pro. Pro. Pro. Pro. 1 D 0 49 product (Fig. 13e) is a substrate for three glycosyl transferases. The sialyl transferase (enzyme 3) produces a trisaccharide (g); a fucosyl transferase produces structure (h) and an N-acetylglucosaminyl transferase produces structure (f). The fucosyl transferase can act also on the sialylated trisaccharide (g) and both fucosylated structures (h) and U) are substrates for an N-acetylgalactosaminyl transferase.

Lys. Asn . Leu. Thr . IX-Lactalbumin (Asn 45 . Gln 46 . ) N'-acetyl Asn. Leu. Ser . Leu. Leu. Tyr. Asn. Leu. Thr. Ser. Val. Tyr. Asp. Leu. Thr . Ser . Val. Tyr. Gin. Leu. Thr. Ser. Val. Tyr. Asn. Leu. Val. Ser. Val. Tyr. Asn . Pro. Thr . Ser . Val. Relative activity (%) 100 473 293 120 5 I 1 100 18 <1 100 o o o o analogous peptides containing glutamine or aspartic acid in place of asparagine are completely inactive. The acceptor requirements for oligosaccharide transfer to polypeptide established by these studies are entirely consistent with the peptide sequences surrounding the glycosylated asparagine residues in glycoproteins [30].

13 Assembly of submaxillary gland glycoproteins. Disallowed reactions are indicated by full lines and partially blocked reactions by broken lines. of the system seem to be similar to the rather exacting requirements of the N-acetylglucosaminyl transferase involved in glycosylation of asparagine residues. Presumably the high proline content of the polypeptides of the submaxillary gland glycoproteins ensures a prolinerich environment around each of the numerous glycosylated hydroxyaminoacid residues in these molecules.

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Glycoproteins by R. Colin Hughes


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