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Mucin-type glycoproteins

Figure 14.2 Representative oligosaccharide structures found on mammalian glycoproteins and glycolipids. The complex oligosaccharides may be bi-, tri-, or tetra-antennary the branches may be more or less elongated with 1—>4 linked lactosamine units, and they may or may not be sialylated. The SLex, Lea, and Leb structures represent the different blood group determinants often present on lipids, and the elongated core 2 structure is a mucin-type glycosylation. Proteoglycans have a common core to which a variety of linear acidic polysaccharides are attached. Figure 14.2 Representative oligosaccharide structures found on mammalian glycoproteins and glycolipids. The complex oligosaccharides may be bi-, tri-, or tetra-antennary the branches may be more or less elongated with 1—>4 linked lactosamine units, and they may or may not be sialylated. The SLex, Lea, and Leb structures represent the different blood group determinants often present on lipids, and the elongated core 2 structure is a mucin-type glycosylation. Proteoglycans have a common core to which a variety of linear acidic polysaccharides are attached.
Strous, G. J. and Dekker, J. Mucin-Type Glycoproteins. Critical Reviews in Biochemistry and Molecular Biology, 1992, 27(2), 57-92. [Pg.232]

Campbell, B.J., Biochemical and Functional Aspects of Mucus and Mucin-type Glycoproteins. In Bioadhesive Drug Delivery Systems (E. Mathiowitz, D.E. Chickering, lit, and C.-M. Lehr, eds.) Marcel Dekker, Inc., New York, 1999, pp. 85-130. [Pg.188]

Because of the numerous methods available for the hydrolysis of various glycoconjugates, including glycoproteins, mucins, glycosaminogly-cans, and gangliosides, it is useful to arrange these methods according to the type of acid employed. Some studies compared a particular method of... [Pg.265]

Htilsmeier, A.J., Gehrig, P.M., Geyer, R., Sack, R., Gottstein, B., Deplazes, P. and Kohler, P. (2002) A major Echinococcus multilocularis antigen is a mucin-type glycoprotein. Journal of Biological Chemistry 277, 5742-5748. [Pg.419]

Qmtoft, T. F., Harving, N., and Langkilde, N. C. 1990. O-linked mucin-type glycoproteins in normal and malignant colon mucosa Lack of T-antigen expression and accumulation of Tn and sialo-syl-Tn antigens in carcinomas. Int. J. Cancer 45 666-672. [Pg.334]

Campbell, B. J. Biochemical and functional aspects of mucus and mucin-type glycoproteins, in Bioadhesive Drug Delivery Systems Fundamentals, Novel Approaches, and Development. New York Marcel Dekker, 1999. [Pg.199]

Carraway, K. and Hull, S. (1991) Cell surface mucin-type glycoproteins and mucin-like domains. Glycobiology 1, 131-138. [Pg.203]

Spiro R.G. (2002). Protein glycosylation nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 12 43R-56R Strous G.J. and Dekker J. (1992) Mucin-type glycoproteins. Crit Rev Biochem Mol Biol 27,... [Pg.48]

The reaction of partially purified, lima-bean lectin with hog gastric-mucin type A substance exemplified the precipitin-like curve obtained for lectin-polysaccharide or -glycoprotein reactions.103 Classical precipitin-curves between purified components II and III and type A blood-group substance were also obtained.151,199 Maximal precipitation of component II (equivalence) occurred at a lower ratio of A substance per mole of protein than for component III. Under conditions where type A substance precipitated 90% of the lectin, types A2 and B precipitated151,199 66 and 13%, respectively, of component II, and 21 and 0% of component III. Neither of the lima-bean lectins precipitated with type O blood-group substance. [Pg.248]

Figure 4 Overview of mucin-type 0-linked glycoprotein biosynthesis. The production of the eight core structures found in 0-glycans is shown along with the enzymes and nucleotide sugars that are involved in each step. Additional information on the enzymes shown can be found in the KEGG databases (see the Legend for Fig. 3). Figure 4 Overview of mucin-type 0-linked glycoprotein biosynthesis. The production of the eight core structures found in 0-glycans is shown along with the enzymes and nucleotide sugars that are involved in each step. Additional information on the enzymes shown can be found in the KEGG databases (see the Legend for Fig. 3).

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See also in sourсe #XX -- [ Pg.188 ]




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