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Oviduct glycoprotein

Kdn-gp appeared to be synthesized during relatively later stages of oogenesis, since it was undetectable in the oocyte 3 months prior to ovulation. Although the cell types that synthesize Kdn-gp have not been identified, it is most likely synthesized under hormonal control in some extraoocj e cells (i.e. follicle cells), secreted and partly incorporated into the second outermost layer of the vitelline envelope just before ovulation. Kdn-gp may thus be a molecule homologous to the oviduct glycoproteins of mammals that are reported to be secreted and partly incorporated into the egg surface [58-60]. [Pg.156]

Buhi WC, Alvarez IM, Choi I, Cleaver BD, Simmen FA 1996 Molecular cloning and characterization of an estrogen-dependent porcine oviductal secretory glycoprotein. Biol Reprod 55 1305-1314... [Pg.192]

Malette, B., Paquette, Y., Merlen, Y. and Bleau, G. (1995) Oviductins possess chitinase and mucin-like domains a lead in the search for biological function of these oviduct-specific ZP-associating glycoproteins. Molecular Reproduction and Development 41, 384-397. [Pg.217]

Sendai, Y., Abe, H., Kikuchi, M., Satoh, T. and Hoshi, H. (1995) Purification and molecular cloning of bovine oviduct specific glycoprotein. Biology of Reproduction 50, 927-934. [Pg.217]

Secretion of nonglycosylated macromolecules in the presence of tunicamycin has also been investigated in a number of other cells. Rat-liver cell-secretion ol albumin (a carbohydrate-free protein), transferrin, and a-acid glycoprotein was not inhibited, and, in chick-liver cells, only a decrease by 10-25% in the secretion of transferrin and the apoprotein B chain of very-low-density lipoprotein was noted.463,464 The secretion of ovalbumin (a glycoprotein) from hen oviduct was not blocked by tunicamycin.465... [Pg.362]

Paul-Gardais, A., Picard, J., Hermelin, B. Turnover of sulfate in glycopeptides from egg shell membranes and hen oviduct sulfated glycoproteins. Biochim. Biophys. Acta 354, 11 (1974)... [Pg.134]

In contrast to sero- and lactotransferrins, glycans of ovotransferrins from avian egg-white contain a bisecting A-acetylglucosamine residue, like other glycoproteins from oviducts, such as ovomucoid and ovalbumin for instance (Fig. 16A-C). Like all of the avian egg glycoproteins, ovotransferrins are not fueosylated. [Pg.223]

I. Brockhausen, J. Carver, H. Schachter, Control of Glycoprotein Synthesis. XIV. The use of oligosaccharide substrates and HPLC to study the sequential pathway for N-acetylglucosa-minyltransferases I, II, III, IV, V and VI in the biosynthesis of highly branched N-glycans by hen oviduct membranes, Biochem Cell Biol, 1988, 66, 1134-1151. [Pg.1290]


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See also in sourсe #XX -- [ Pg.17 , Pg.280 ]




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