Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1972 Jul;128(3):579–586. doi: 10.1042/bj1280579

The subcellular distribution of triphosphoinositide phosphomonoesterase in guinea-pig brain

A Sheltawy 1, M Brammer 1, D Borrill 1
PMCID: PMC1173809  PMID: 4344004

Abstract

1. Some properties of the triphosphoinositide phosphomonoesterase from the homogenates of guinea-pig brain were studied. The enzyme has an optimum pH range 6.7–7.3, is stimulated with KCl at a concentration of 0.1m, and under these conditions has Km1.43×10−4m. 2. A factor from the `pH5 supernatant' of guinea-pig brain stimulates the enzyme activity over and above the stimulation produced by KCl. Subcellular fractions of guinea-pig brain varied in their response to the `pH5 supernatant'. Maximum stimulation was observed with the P1 fraction, containing myelin and nuclei. 3. An assay system for the enzyme was developed that contained optimum concentrations of both KCl and the `pH5 supernatant'. Acid phosphatases were inhibited by NaF, but, in contrast with previous work, no EDTA was added to the assay system to inhibit the alkaline phosphatases. This reagent inhibited the triphosphoinositide phosphomonoesterase. It was estimated that the remaining fraction of non-specific phosphatases can account for only 14% of the observed triphosphoinositide phosphomonoesterase activity. 4. Subcellular fractions of guinea-pig brain were characterized by electron microscopy and subcellular markers. The triphosphoinositide phosphomonoesterase exhibited a distribution between the fractions similar to that of 5′-nucleotidase, but different from that of alkaline phosphatase.

Full text

PDF
579

Selected References

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

  1. BLIGH E. G., DYER W. J. A rapid method of total lipid extraction and purification. Can J Biochem Physiol. 1959 Aug;37(8):911–917. doi: 10.1139/o59-099. [DOI] [PubMed] [Google Scholar]
  2. DITTMER J. C., DAWSON R. M. The isolation of a new lipid, triphosphoinositide, and monophosphoinositide from ox brain. Biochem J. 1961 Dec;81:535–540. doi: 10.1042/bj0810535. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dawson R. M., Thompson W. The triphosphoinositide phosphomonoesterase of brain tissue. Biochem J. 1964 May;91(2):244–250. doi: 10.1042/bj0910244. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Eichberg J., Dawson R. M. Polyphosphoinositides in myelin. Biochem J. 1965 Sep;96(3):644–650. doi: 10.1042/bj0960644. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Eichberg J., Whittaker V. P., Dawson R. M. Distribution of lipids in subcellular particles of guinea-pig brain. Biochem J. 1964 Jul;92(1):91–100. doi: 10.1042/bj0920091. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gonzalez-Sastre F., Folch-Pi J. Thin-layer chromatography of the phosphoinositides. J Lipid Res. 1968 Jul;9(4):532–533. [PubMed] [Google Scholar]
  7. Harwood J. L., Hawthorne J. N. Metabolism of the phosphoinositides in guinea-pig brain synaptosomes. J Neurochem. 1969 Sep;16(9):1377–1387. doi: 10.1111/j.1471-4159.1969.tb05989.x. [DOI] [PubMed] [Google Scholar]
  8. Kai M., Hawthorne J. N. Incorporation of injected [32P] phosphate into the phosphoinositides of subcellular fractions from young rat brain. Biochem J. 1966 Jan;98(1):62–67. doi: 10.1042/bj0980062. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kai M., Salway J. G., Hawthorne J. N. The diphosphoinositide kinase of rat brain. Biochem J. 1968 Feb;106(4):791–801. doi: 10.1042/bj1060791. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kai M., White G. L., Hawthorne J. N. The phosphatidylinositol kinase of rat brain. Biochem J. 1966 Nov;101(2):328–337. doi: 10.1042/bj1010328. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Keough K. M., Thompson W. Triphosphoinositide phosphodiesterase in developing brain of the rat and in subcellular fractions of brain. J Neurochem. 1970 Jan;17(1):1–11. doi: 10.1111/j.1471-4159.1970.tb00495.x. [DOI] [PubMed] [Google Scholar]
  12. 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]
  13. Lee T. C., Huggins C. G. Triphosphoinositide phosphomonoesterase in rat kidney cortex. I. General properties and subcellular localization. Arch Biochem Biophys. 1968 Jul;126(1):206–213. doi: 10.1016/0003-9861(68)90575-4. [DOI] [PubMed] [Google Scholar]
  14. Michell R. H., Hawthorne J. N. The site of diphosphoinositide synthesis in rat liver. Biochem Biophys Res Commun. 1965 Nov 22;21(4):333–338. doi: 10.1016/0006-291x(65)90198-1. [DOI] [PubMed] [Google Scholar]
  15. Palmer F. B., Dawson R. M. Complex-formation between triphosphoinositide and experimental allergic encephalitogenic protein. Biochem J. 1969 Mar;111(5):637–645. [PubMed] [Google Scholar]
  16. Salway J. G., Kai M., Hawthorne J. N. Triphosphoinositide phosphomonoesterase activity in nerve cellbodies, neuroglia and subcellular fractions from whole rat brain. J Neurochem. 1967 Oct;14(10):1013–1024. doi: 10.1111/j.1471-4159.1967.tb09512.x. [DOI] [PubMed] [Google Scholar]
  17. Sheltawy A., Dawson R. M. The deposition and metabolism of polyphosphoinositides in rat and guinea-pig brain during development. Biochem J. 1969 Jan;111(2):147–154. doi: 10.1042/bj1110147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Sheltawy A., Dawson R. M. The metabolism of polyphosphoinositides in hen brain and sciatic nerve. Biochem J. 1969 Jan;111(2):157–165. doi: 10.1042/bj1110157. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Sheltawy A., Dawson R. M. The polyphosphoinositides and other lipids of peripheral nerves. Biochem J. 1966 Jul;100(1):12–18. doi: 10.1042/bj1000012. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Thompson W., Dawson R. M. The triphosphoinositide phosphodiesterase of brain tissue. Biochem J. 1964 May;91(2):237–243. doi: 10.1042/bj0910237. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Thuneberg L., Rostgaard J. Isolation of brush border fragments from homogenates of rat and rabbit kidney cortex. Exp Cell Res. 1968 Jul;51(1):123–140. doi: 10.1016/0014-4827(68)90163-8. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES