Summary
A fetuin, fucosyl transferase has been identified in the smooth microsomal fraction from the rat exocrine pancreas. This enzyme is involved in the glycosylation of secretory proteins and is bound to membranes, predominantly of the Golgi complex. Optimal in vitro conditions for the assay of the enzyme activity were established: a pH of 5.5–6.0, a temperature of 21° C and concentrations of Mg+ + at 5.0 mM and ATP at 2.0 mM.
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References
Bella, A., Kim, V.S.: Biosynthesis of intestinal glycoprotein: A study of an (1–2) fucosyltransferase in rat small intestinal mucosa. Arch. Biochem. Biophys. 147, 753–761 (1971)
Bieger, W., Seybold, J., Kern, H.F.: Studies on intracellular transport of secretory proteins in the rat exocrine pancreas. V. Kinetic studies on accelerated transport following caerulein infusion in vivo. Cell Tiss. Res. 170, 203–219 (1976)
Bosmann, H.B., Hagopian, A., Eylar, E.H.: Glycoprotein biosynthesis: The characterization of two glycoprotein: fucosyl transferases in Hela cells. Arch. Biochem. Biophys. 128, 470–481 (1968)
Carlson, D.M., David, J., Rütter, W.J.: Galactosyltransferase activities in pancreas, liver and gut of the developing rat. Arch. Biochem. Biophys. 157, 605–612 (1973)
Lewis, D.S., MacDonald, R.J., Kronquist, W.E., Ronzio, R.A.: Purification and partial characterization of an integral membrane glycoprotein from zymogen granules of dog pancreas. FEBS Letters 76, 115–120 (1977)
Lowry, O.H., Rosenbrough, N.J., Farr, A.L., Randell, R.J.: Protein measurement with the Folin phenol reagent. J. biol. Chem. 193, 265–275 (1951)
MacDonald, R.J., Ronzio, R.A.: Comparative analysis of zymogen granule membrane polypeptides. Biochem. biophys. Res. Commun. 49, 377–382 (1972)
Ronzio, R.A.: Glycoprotein synthesis in the adult rat pancreas. I. Subcellular distributions of uridine diphosphate galactose: glycoprotein galactosyltransferase and thiamine pyrophosphate phosphohydrolase. Biochim. biophys. Acta (Amst.) 313, 286–295 (1973)
Schachter, H.: Glycosylation of glycoproteins during inracellular transport of secretory products. In: Advances in cytopharmacology (B. Ceccarelli, F. Clementi, J. Meldolesi, eds.), Vol. 2, pp 207–217. New York; Raven Press 1974
Scheele, G.A., Palade, G.E.: Studies on guinea pig pancreas. Parallel discharge of exocrine enzyme activities. J. biol. Chem. 250, 2660–2670 (1975)
Spiro, A.G.: Studies on fetuin, a glycoprotein of fetal serum. I. J. biol. Chem. 235, 2860–2869 (1960)
Tartakoff, A.M., Jamieson, J.D.: Subcellular fractionation of the pancreas. In: Methods in enzymology (eds. S. Fleischer and L. Packer), Vol. 31, pp. 41–59. New York: Academic Press 1974
Völkl, A., Bieger, W., Kern, H.F.: Studies on secretory glycoproteins in the rat exocrine pancreas. I. Fine structure of the Golgi complex and release of fucose-labeled proteins after in vivo stimulation with caerulein. Cell Tiss. Res. 175, 227–243 (1976)
Völkl, A., Seybold, J., Kern, H.F.: Studies on secretory glycoproteins in the rat exocrine pancreas. III. Evaluation of intracellular transport of both regular and fucosylated secretory proteins by means of cell fractionation. (In preparation, 1978)
Whaley, W.G.: The Golgi apparatus. Cell biology monographs, Vol. 2, Berlin-Heidelberg-New York: Springer 1975
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Supported by a grant from the Deutsche Forschungsgemeinschaft, Bonn-Bad Godesberg (Ke 113/10). Dedicated to Professor Helmut Ferner, Vienna, on the occasion of his 65th birthday.
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Völkl, A., Seybold, J. & Kern, H.F. Studies on secretory glycoproteins in the rat exocrine pancreas. Cell Tissue Res. 186, 111–119 (1978). https://doi.org/10.1007/BF00219658
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DOI: https://doi.org/10.1007/BF00219658