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Cell Glycoprotein

Davis, S. J., Greene, A., LuUau, E. and Abbott, W. M. (1993). Expression of soluble recombinant glycoproteins with predefined glycosylation appUcation to the crystallization of the T-cell glycoprotein CD2. Protein Eng. 6, 229-232. [Pg.42]

Brennan MJ, David JL, Kenimer JG, etal. (1988) Binding of pertussis toxin to a 165-kilodalton Chinese hamster ovary cell glycoprotein. In J. Biol. Chem. 263 4895-4899. [Pg.46]

Howard, R. J., Haynes, J. D., McGinniss, M. H., and Miller, L. H. (1982b). Studies on the role of red blood cell glycoproteins as receptors for invasion by Plasmodium falciparum mer-ozoites. Mol. Biochem. Parasitol. 6,303-315. [Pg.351]

Sialic acid (NANA), other amino sugars Glutamine Most cells In the liver, synthesis of oligosaccharide chains on secreted proteins. Most cells, glycoproteins, proteoglycans, and glycolipids. [Pg.850]

Various structural features of proteins, such as polypeptide size and net charge, are known to influence their in vivo degradative rates. The presence of covalently bound carbohydrate has been shown to be a third feature of protein structure that correlates with protein half-lives within cells.Glycoproteins have been found to be degraded more rapidly than unfractionated proteins or fractions enriched for non-glycoproteins in rat liver, muscle, brain, and kidney, and also in human fibroblasts grown in culture. [Pg.366]

Forstner, J. Taichman, N. Kalnins, V. Forstner, G. Intestinal goblet cell mucus Isolation and identification by immunofluorescence of a goblet cell glycoprotein. J. Cell Sci. 1973,12 (2), 585. [Pg.1249]

Figure 8 shows that such chimeric enzymes are all fully active when expressed in CHO cells. All variants are able to be active on cell glycoproteins without disturbing cell growth and adhesion. When stably transfected, they were shown to be highly active on cell surface proteins, indicating that they may facilitate protein secretion as well. [Pg.502]

Kimo A, Itakura Y, Toyoda M, Takahashi Y, Yamada M, Umezawa A, Hirabayashi J (2008) Developmoit of a data-nuning system for differential profiling of cell glycoproteins based on lectin miCToarray. J Proteonucs Bioinform 1 68—72... [Pg.122]


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