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. 1977 Aug;74(8):3222–3225. doi: 10.1073/pnas.74.8.3222

Unequivocal demonstration of fructose-1,6-bisphosphatase in mammalian brain.

A L Majumder, F Eisenberg Jr
PMCID: PMC431505  PMID: 20624

Abstract

Fructose-1,6-bisphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrolase; EC 3.1.3.11) has been found in rat brain and identified unequivocally. The enzyme has been purified to 95% homogeneity by standard procedures, including adsorption to a phosphocellulose column followed by elution with substrate. The purified enzyme exhibits a broad optimum above pH 7.6. Both fructose 1,6-bisphosphate and sedoheptulose 1,7-bisphosphate are substrates of this enzyme; the hydrolysis of the latter occurs at about 20% of the rate of the former, and the Km for fructose 1,6-bisphosphate is approximately 1.32 X 10(-4) M. 5'-AMP, an inhibitor of other mammalian-fructose-1,6-bisphosphatases, is without effect, and in further contrast with the other enzymes there is no metal requirement for activity. Purified brain enzyme fails to crossreact with the antibody prepared against the purified liver fructose-1,6-bisphosphatase. On the other hand, antiserum produced against the brain fructose-1,6-bisphosphatase quantitatively precipitates the enzyme activity and forms precipitin bands with preparations of brain fructose-1,6-bisphosphatase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Cohen H. J., Harris T. M., Geller A. M., Byrne W. L. Bovine hepatic fructose 1,6-diphosphatase: -glycerophosphate hydrolysis-evidence for a shared active site. Arch Biochem Biophys. 1971 Sep;146(1):144–152. doi: 10.1016/s0003-9861(71)80050-4. [DOI] [PubMed] [Google Scholar]
  2. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  3. Han P. F., Murthy V. V., Johnson J., Jr Chicken liver fructose 1,6-bisphosphatase:purfication and some properties. Arch Biochem Biophys. 1976 Mar;173(1):293–300. doi: 10.1016/0003-9861(76)90262-9. [DOI] [PubMed] [Google Scholar]
  4. Han P. F., Owen G. S., Johnson J., Jr Purification and properties of fructose 1,6-bisphosphatase from turkey liver. Arch Biochem Biophys. 1975 May;168(1):171–179. doi: 10.1016/0003-9861(75)90239-8. [DOI] [PubMed] [Google Scholar]
  5. KREBS H. A., WOODFORD M. FRUCTOSE 1, 6-DIPHOSPHATASE IN STRIATED MUSCLE. Biochem J. 1965 Feb;94:436–445. doi: 10.1042/bj0940436. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  7. Majumder A. L., Eisenberg F., Jr Inhibition of glycolysis in brain by a phospholipid effect on interconversion of fructose phosphates. A possible regulatory control on utilization of glucose 6-phosphate. J Biol Chem. 1976 Nov 25;251(22):7149–7156. [PubMed] [Google Scholar]
  8. Newsholme E. A., Crabtree B., Higgins S. J., Thornton S. D., Start C. The activities of fructose diphosphatase in flight muscles from the bumble-bee and the role of this enzyme in heat generation. Biochem J. 1972 Jun;128(1):89–97. doi: 10.1042/bj1280089. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Phillips M. E., Coxon R. V. Incorporation of isotopic carbon into cerebral glycogen from non-glucose substrates. Biochem J. 1975 Jan;146(1):185–189. doi: 10.1042/bj1460185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Pontremoli S., Traniello S., Luppis B., Wood W. A. Fructose diphosphatase from rabbit liver. I. Purification and properties. J Biol Chem. 1965 Sep;240(9):3459–3463. [PubMed] [Google Scholar]
  11. Ramadoss C. S., Luby L. J., Uyeda K. Affinity chromatography of phosphofructokinase. Arch Biochem Biophys. 1976 Aug;175(2):487–494. doi: 10.1016/0003-9861(76)90536-1. [DOI] [PubMed] [Google Scholar]
  12. Ramadoss C. S., Uyeda K., Johnston J. M. Studies on the fatty acid inactivation of phosphofructokinase. J Biol Chem. 1976 Jan 10;251(1):98–107. [PubMed] [Google Scholar]
  13. Taketa K., Watanabe A., Sarngadharan M. G., Pogell B. M. Reversible, pH-dependent formation of a conformer of rabbit liver fructose 1,6-diphosphatase with low catalytic activity. Biochemistry. 1971 Feb 16;10(4):565–569. doi: 10.1021/bi00780a004. [DOI] [PubMed] [Google Scholar]
  14. Tejwani G. A., Pedrosa F. O., Pontremoli S., Horecker B. L. The purification of properties of rat liver fructose 1,6-bisphosphatase. Arch Biochem Biophys. 1976 Nov;177(1):253–264. doi: 10.1016/0003-9861(76)90435-5. [DOI] [PubMed] [Google Scholar]
  15. Traniello S., Pontremoli S., Tashima Y., Horecker B. L. Fructose 1, 6-diphosphatase from liver: isolation of the native form with optimal activity at neutral pH. Arch Biochem Biophys. 1971 Sep;146(1):161–166. doi: 10.1016/s0003-9861(71)80052-8. [DOI] [PubMed] [Google Scholar]
  16. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

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