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Purification and Properties of Phosphofructokinase 2/fructose 2,6-bisphosphatase From Chicken Liver and From Pigeon Muscle

  1. CLAUS T.H., EL-MAGHRABI M.R., REGEN D.M., STEWART H.B., MCGRANE M., KOUNTZ P.D., NYFELER F., PILKIS J., PILKIS S.J., The Role of Fructose 2,6-Bisphosphate in the Regulation of Carbohydrate Metabolism, Current Topics in Cellular Regulation (1984) ISBN:9780121528232 p.57-86, 10.1016/b978-0-12-152823-2.50006-4
  2. Schaftingen E., Adv. Enzymol. Relat. Areas Mol. Biol., 59 (1986)
  3. Sener A, Van Schaftingen E, Van de Winkel M, Pipeleers D G, Malaisse-Lagae F, Malaisse W J, Hers H G, Effects of glucose and glucagon on the fructose 2,6-bisphosphate content of pancreatic islets and purified pancreatic B-cells. A comparison with isolated hepatocytes, 10.1042/bj2210759
  4. Hue L., J. Biol. Chem., 257, 4308 (1982)
  5. Rider M H, Foret D, Hue L, Comparison of purified bovine heart and rat liver 6-phosphofructo-2-kinase. Evidence for distinct isoenzymes, 10.1042/bj2310193
  6. Francois J., Eur. J. Biochem., 145, 187 (1984)
  7. Schaftingen E., Eur. J. Biochem., 159, 367 (1986)
  8. Schaftingen E., Eur. J. Biochem., 129, 191 (1982)
  9. Schaftingen E., Eur. J. Biochem., 117, 319 (1981)
  10. Schaftingen E., Eur. J. Biochem., 124, 143 (1982)
  11. Walseth Timothy F., Johnson Roger A., The enzymatic preparation of [α-32P]nucleoside triphosphates, cyclic [32P]AMP, and cyclic [32P]GMP, 10.1016/0005-2787(79)90122-9
  12. Van Schaftingen Emile, Hers Henri-Géry, Fructose 2,6-bisphosphate in relation with the resumption of metabolic activity in slices of Jerusalem artichoke tubers, 10.1016/0014-5793(83)80048-9
  13. Roskoski Robert, [1] Assays of protein kinase, Methods in Enzymology (1983) ISBN:9780121819996 p.3-6, 10.1016/0076-6879(83)99034-1
  14. Schaftingen E., Biochem. Biophys. Res. Commun., 103, 362 (1981)
  15. Lowry O. H., J. Biol. Chem., 19, 265 (1951)
  16. Bradford M, A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding, 10.1006/abio.1976.9999
  17. Buss J. E., Methods Enzymol., 99, 7 (1983)
  18. Laemmli U. K., Nature (Lond.), 227, 680 (1970)
  19. Wray Wayne, Boulikas Teni, Wray Virginia P., Hancock Ronald, Silver staining of proteins in polyacrylamide gels, 10.1016/0003-2697(81)90179-2
  20. Pilkis S. J., J. Biol. Chem., 258, 6135 (1983)
  21. Pilkis S. J., J. Biol. Chem., 259, 949 (1984)
  22. Stewart H. B., J. Biol. Chem., 260, 12935 (1985)
  23. El-Maghrabi M. R., Biochem. Biophys. Res. Commun., 106, 794 (1982)
  24. Sakakibara R., J. Biol. Chem., 259, 41 (1984)
  25. Laloux M., Eur. J. Biochem., 148, 155 (1985)
  26. Murray K. J., J. Biol. Chem., 259, 7673 (1984)
  27. El-Maghrabi M. R., Biochem. Biophys. Res. Commun., 123, 749 (1984)
  28. Van Schaftingen E, Bartrons R, Hers H G, The mechanism by which ethanol decreases the concentration of fructose 2,6-bisphosphate in the liver, 10.1042/bj2220511
  29. Hultquist D.E., The preparation and characterization of phosphorylated derivatives of histidine, 10.1016/0005-2728(68)90078-9
  30. Rose Z. B., Arch. Biochem. Biophys., 140, 508 (1970)
  31. Lackner R, Challiss R A J, West D, Newsholme E A, A problem in the radiochemical assay of glucose-6-phosphatase in muscle, 10.1042/bj2180649
  32. Hunter F.R., Facilitated diffusion in erythrocytes of additional mammals, 10.1016/0300-9629(76)90054-2
  33. Chaekal O. K., Arch. Biochem. Biophys., 225, 771 (1983)
  34. Ochs R. S., Arch. Biochem. Biophys., 190, 193 (1978)
Bibliographic reference Van Schaftingen, Emile ; Hers, HG.. Purification and Properties of Phosphofructokinase 2/fructose 2,6-bisphosphatase From Chicken Liver and From Pigeon Muscle. In: European Journal of Biochemistry, Vol. 159, no. 2, p. 359-365 (1986)
Permanent URL http://hdl.handle.net/2078.1/54353