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Glycosylation function

Many enzymes are known which will transfer glycosyl functions specifically to receptor hydroxy compounds, but although this possibility offers means for obtaining specific glycosides it has not been used extensively, largely because the techniques are unfamiliar to the organic chemist and because they are not well suited to the preparation of large amoimts of materials. Pridham has surveyed the enzymic reactions... [Pg.53]

Structure—function relationships of prolactin among a variety of species have been pubUshed (17,18). Only one gene for prolactin appears to exist (19). Although classically placed in the category of simple protein hormones, prolactin can be glycosylated. Carbohydrate attachment occurs at Asn-31, where the consensus glycosylation sequence Asn—X—Ser is found. [Pg.176]

Prolactin-Like Proteins. A number of prolactin-like proteins (PLPs), which ate distinct from the PLs, have been identified in mminants and rodents (11,23). Several cDNA transcripts coding for PLPs in catde have been identified (23). These transcripts code for proteins which possess about 40% sequence homology with bovine PRL 60% if conservative substitutions ate considered. Three glycosylated PLPs, ie, PLP-A, -B, and -C, ate produced during pregnancy in the rat (11). Two additional prolactin-related molecules have been identified in the mouse (24,25), ie, proliferin [92769-12-5] (PLF) and PLF-related protein [98724-27-7]. These ate not found in other rodents and may be unique to the mouse. The functional roles of PLPs remain to be deterrnined. [Pg.183]

Evolution has provided the cell with a repertoire of 20 amino acids to build proteins. The diversity of amino acid side chain properties is enormous, yet many additional functional groups have been selectively chosen to be covalently attached to side chains and this further increases the unique properties of proteins. Diese additional groups play a regulatory role allowing the cell to respond to changing cellular conditions and events. Known covalent modifications of proteins now include phosphorylation, methylation, acetylation, ubi-quitylation, hydroxylation, uridylylation and glycosyl-ation, among many others. Intense study in this field has shown the addition of a phosphate moiety to a protein... [Pg.1023]

Of the many methods described for glycoside synthesis, those predominantly used in current oligosaccharide synthesis, in which the glycosyl donor has O- or N- functionality at C-2 (that is, excluding 2-deoxyglycosides), are the following ... [Pg.180]

An alternative could be steric activation-deactivation at the anomeric centers of the donor and acceptor. An example using this concept is shown in Scheme 12. In the electronic activation-deactivation concept, deactivated p-nitrophenyl thioglycosides can, after functioning as glycosyl acceptors, be transformed into... [Pg.190]

Venom Allergen Function/ name MW kDa Major/ minor Cloned and sequenced Expressed as recombinant Glycosylated (n sites)... [Pg.145]


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Functional groups glycosylation process

Functions of Glycosyl Phosphatidylinositols

Participation by Functional Groups in the Glycosyl Donor

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