Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1965 Aug;96(2):404–412. doi: 10.1042/bj0960404

The localization of adenosine triphosphatases in morphologically characterized subcellular fractions of guinea-pig brain

R Jeanette A Hosie 1,*
PMCID: PMC1207054  PMID: 4220903

Abstract

1. The distribution of adenosine triphosphatase was studied in morphologically characterized subcellular fractions of guinea-pig brain. The conditions of homogenization were selected so as to favour the survival of nerve endings as organized structures. 2. A fraction consisting mainly of the external membranes of nerve endings was rich in a ouabain-sensitive Na+–K+-stimulated adenosine triphosphatase which closely resembled that present in the classical microsomal fraction studied by other workers, but which showed a higher specific activity. 3. A dinitrophenol-stimulated adenosine triphosphatase was located in the nerve-ending mitochondria. 4. The synaptic-vesicle fraction contained a small amount of adenosine triphosphatase that differed in its response to several ions and other compounds from the membrane, myelin and mitochondrial fractions, indicating freedom from contamination by these elements.

Full text

PDF
404

Images in this article

408-1PLATE 1
on p.408-1
408-2PLATE 2
on p.408-2

Selected References

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

  1. ALDRIDGE W. N. Adenosine triphosphatase in the microsomal fraction from rat brain. Biochem J. 1962 Jun;83:527–533. doi: 10.1042/bj0830527. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. ALDRIDGE W. N., EMERY R. C., STREET B. W. A tissue homogenizer. Biochem J. 1960 Nov;77:326–327. doi: 10.1042/bj0770326. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. AUTILIO L. A., NORTON W. T., TERRY R. D. THE PREPARATION AND SOME PROPERTIES OF PURIFIED MYELIN FROM THE CENTRAL NERVOUS SYSTEM. J Neurochem. 1964 Jan;11:17–27. doi: 10.1111/j.1471-4159.1964.tb06719.x. [DOI] [PubMed] [Google Scholar]
  4. BONTING S. L., CARAVAGGIO L. L., HAWKINS N. M. Studies on sodium-potassium-activated adenosinetriphosphatase. IV. Correlation with cation transport sensitive to cardiac glycosides. Arch Biochem Biophys. 1962 Sep;98:413–419. doi: 10.1016/0003-9861(62)90206-0. [DOI] [PubMed] [Google Scholar]
  5. CUMMINS J., HYDEN H. Adenosine triphosphate levels and adenosine triphosphatases in neurons, glia and neuronal membranes of the vestibular nucleus. Biochim Biophys Acta. 1962 Jul 2;60:271–283. doi: 10.1016/0006-3002(62)90403-1. [DOI] [PubMed] [Google Scholar]
  6. DEUL D. H., McILWAIN H. Activation and inhibition of adenosine triphosphatases of subcellular particles from the brain. J Neurochem. 1961 Dec;8:246–256. doi: 10.1111/j.1471-4159.1961.tb13550.x. [DOI] [PubMed] [Google Scholar]
  7. DUNHAM E. T., GLYNN I. M. Adenosinetriphosphatase activity and the active movements of alkali metal ions. J Physiol. 1961 Apr;156:274–293. doi: 10.1113/jphysiol.1961.sp006675. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. EMMELOT P., BOS C. J. Adenosine triphosphatase in the cell-membrane fraction from rat liver. Biochim Biophys Acta. 1962 Apr 9;58:374–375. doi: 10.1016/0006-3002(62)91031-4. [DOI] [PubMed] [Google Scholar]
  9. ERNSTER L., LINDBERG O. Determination of organic phosphorus compounds by phosphate analysis. Methods Biochem Anal. 1956;3:1–22. doi: 10.1002/9780470110195.ch1. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. GLYNN I. M. TRANSPORT ADENOSINETRIPHOSPHATASE' IN ELECTRIC ORGAN. THE RELATION BETWEEN ION TRANSPORT AND OXIDATIVE PHOSPHORYLATION. J Physiol. 1963 Nov;169:452–465. doi: 10.1113/jphysiol.1963.sp007272. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. GORE M. B. R. Adenosinetriphosphatase activity of brain. Biochem J. 1951 Nov;50(1):18–24. doi: 10.1042/bj0500018. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. HESS H. H., POPE A. Intralaminar distribution of adenosinetriphosphatase activity in rat cerebral cortex. J Neurochem. 1959 Feb;3(4):287–299. doi: 10.1111/j.1471-4159.1959.tb12635.x. [DOI] [PubMed] [Google Scholar]
  14. JARNEFELT J. Sodium-stimulated adenosinetriphosphatase in microsomes from rat brain. Biochim Biophys Acta. 1961 Mar 18;48:104–110. doi: 10.1016/0006-3002(61)90520-0. [DOI] [PubMed] [Google Scholar]
  15. LEWIN E., HESS H. H. INTRALAMINAR DISTRIBUTION OF NA+-K+ ADENOSINE TRIPHOSPHATASE IN RAT CORTEX. J Neurochem. 1964 Jun;11:473–481. doi: 10.1111/j.1471-4159.1964.tb11606.x. [DOI] [PubMed] [Google Scholar]
  16. LUFT J. H. Permanganate; a new fixative for electron microscopy. J Biophys Biochem Cytol. 1956 Nov 25;2(6):799–802. doi: 10.1083/jcb.2.6.799. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. MICHAELSON I. A., WHITTAKER V. P. The subcellular localization of 5-hydroxytryptamine in guinea pig brain. Biochem Pharmacol. 1963 Feb;12:203–211. doi: 10.1016/0006-2952(63)90185-0. [DOI] [PubMed] [Google Scholar]
  18. MILLONIG G. A modified procedure for lead staining of thin sections. J Biophys Biochem Cytol. 1961 Dec;11:736–739. doi: 10.1083/jcb.11.3.736. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. POST R. L., MERRITT C. R., KINSOLVING C. R., ALBRIGHT C. D. Membrane adenosine triphosphatase as a participant in the active transport of sodium and potassium in the human erythrocyte. J Biol Chem. 1960 Jun;235:1796–1802. [PubMed] [Google Scholar]
  20. SCHWARTZ A., BACHELARD H. S., McIL WAIN H. The sodium-stimulated adenosine-triphosphatase activity and other properties of cerebral microsomal fractions and subfractions. Biochem J. 1962 Sep;84:626–637. doi: 10.1042/bj0840626. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. SKOU J. C. Preparation from mammallian brain and kidney of the enzyme system involved in active transport of Na ions and K ions. Biochim Biophys Acta. 1962 Apr 9;58:314–325. doi: 10.1016/0006-3002(62)91015-6. [DOI] [PubMed] [Google Scholar]
  22. SKOU J. C. Studies on the Na ion and K ion activated ATP hydrolysing enzyme system. The role of SH groups. Biochem Biophys Res Commun. 1963 Jan 18;10:79–84. doi: 10.1016/0006-291x(63)90272-9. [DOI] [PubMed] [Google Scholar]
  23. SOMOGYI J. UBER DIE WIRKUNG DER CA-IONEN AUF DIE DURCH NA+ UND K+ AKTIVIERBARE ADENOSINTRIPHOSPHATASE DES HIRNGEWEBES. Hoppe Seylers Z Physiol Chem. 1964;336:264–270. doi: 10.1515/bchm2.1964.336.1.264. [DOI] [PubMed] [Google Scholar]
  24. WHITTAKER V. P., DOWE G. H. THE EFFECT OF HOMOGENIZATION CONDITIONS ON SUB-CELLULAR DISTRIBUTION IN BRAIN. Biochem Pharmacol. 1965 Feb;14:194–196. doi: 10.1016/0006-2952(65)90081-x. [DOI] [PubMed] [Google Scholar]
  25. WHITTAM R. Active cation transport as a pace-maker of respiration. Nature. 1961 Aug 5;191:603–604. doi: 10.1038/191603a0. [DOI] [PubMed] [Google Scholar]
  26. Wheeler K. P., Whittam R. Structural and enzymic aspects of the hydrolysis of adenosine triphosphate by membranes of kidney cortex and erythrocytes. Biochem J. 1964 Nov;93(2):349–363. doi: 10.1042/bj0930349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Whittaker V. P., Michaelson I. A., Kirkland R. J. The separation of synaptic vesicles from nerve-ending particles ('synaptosomes'). Biochem J. 1964 Feb;90(2):293–303. doi: 10.1042/bj0900293. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES