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Asparagine glycosylation

Runge, K. W., Huffaker, T. C., and Robbins, P. W. (1984). Two yeast mutations in gluco-sylation steps of the asparagine glycosylation pathway. / Biol. Chem. 259, 412-417. [Pg.387]

Glycosydation AChE and BChE carry 3 and 9, respectively, N-glycosylation consensus sequences attaching carbohydrate residues to the core protein via asparagines. Different molecular forms of the enzymes in various tissues, show different number and composition of carbohydrate residues. N-glycosylation at all sites was shown to be important for effective biosynthesis, secretion and clearance of ChEs from the circulation. Altered patterns of AChE glycosylation have been observed in the brain and cerebrospinal fluid of Alzheimer s disease (AD) patients, with potential diagnostic value. [Pg.359]

Rituximab is a recombinant mouse/human chimeric monoclonal antibody whose in vitro activity varies with the number of terminal galactose moieties glycosylated to the peptide backbone at residue asparagine 301 [8]. The ability to monitor the levels of each discrete species present would allow the manufacturing process to... [Pg.201]

Fig. 3. (A) Disposition of afi unit in the membrane, based on sequence information [14,15], selective proteolytic digestion of the a subunit [5,6] and hydrophobic labelling (Table 1). The model for the (S subunit is based on sequencing of surface peptides and identification of S-S bridges [64,65]. T, T2 and C3 show location of proteolytic splits. CHO are glycosylated asparagines in the P subunit. (B) Peptide fragments remaining in the membrane after extensive tryptic digestion of membrane-bound Na,K-ATPase from outer medulla of pig kidney as described by Karlish et al. [7,58]. Fig. 3. (A) Disposition of afi unit in the membrane, based on sequence information [14,15], selective proteolytic digestion of the a subunit [5,6] and hydrophobic labelling (Table 1). The model for the (S subunit is based on sequencing of surface peptides and identification of S-S bridges [64,65]. T, T2 and C3 show location of proteolytic splits. CHO are glycosylated asparagines in the P subunit. (B) Peptide fragments remaining in the membrane after extensive tryptic digestion of membrane-bound Na,K-ATPase from outer medulla of pig kidney as described by Karlish et al. [7,58].
The physical properties of the synthetic glycosyl derivatives of l-asparagine, L-serine, and L-threonine are reported in Tables I-V. Derivatives characterized otherwise, but without m.p. and optical rotation, have also been included. Whenever more than one reference is given, the physical constants are taken from the references printed in bold letters. The abbreviations used in the m.p. column are as follows foam., foaming dec., decomposing and soft., softening. [Pg.181]

A number of the central themes of current glycoconjugate research can be traced back to studies begun in the Jeanloz laboratory. One prominent example is the elucidation of the sequences of the carbohydrates linked N- or O-glycosylically to asparagine or serine/threonine residues respectively in glycoproteins. Little was... [Pg.11]

Urge, L., Otvos Jr., L., Lang, E., Wroblewski, K., Laczko, I., and Hollosi, M. (1992) Fmoc-protected, glycosylated asparagines potentially useful as reagents in the solid-phase synthesis of N-glycopeptides. Carbohydr. Res. 235, 83-93. [Pg.1123]

Human a-galactosidase is a 100 kDa homodimeric glycoprotein. Each 398 amino acid monomer displays a molecular mass of 45.3 kDa (excluding the glycocomponent) and is glycosylated at three positions (asparagines 108, 161 and 184). After administration (usually every second week by a 40 min infusion), the enzyme is taken up by various body cell types and directed to the lysosomes. This cellular uptake and delivery process appear to be mediated by mannose-... [Pg.360]

DEVELOPMENTS IN THE SYNTHESIS OF GLYCOPEPTIDES CONTAINING GLYCOSYL l-ASPARAGINE, l-SERINE, AND... [Pg.277]


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