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. 1962 Sep;84(3):626–637. doi: 10.1042/bj0840626

The sodium-stimulated adenosine-triphosphatase activity and other properties of cerebral microsomal fractions and subfractions

A Schwartz 1, H S Bachelard 1, H McIlwain 1
PMCID: PMC1243724  PMID: 13909665

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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., JOHNSON M. K. Cholinesterase, succinic dehydrogenase, nucleic acids, esterase and glutathione reductase in sub-cellular fractions from rat brain. Biochem J. 1959 Oct;73:270–276. doi: 10.1042/bj0730270. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. BARBATO I. M., ALPERT N. R. The preparation and characteristics of a purified muscle adenosinetriphosphatase. Arch Biochem Biophys. 1961 May;93:255–261. doi: 10.1016/0003-9861(61)90259-4. [DOI] [PubMed] [Google Scholar]
  4. BONTING S. L., SIMON K. A., HAWKINS N. M. Studies on sodium-potassium-activated adenosine triphosphatase. I. Quantitative distribution in several tissues of the cat. Arch Biochem Biophys. 1961 Dec;95:416–423. doi: 10.1016/0003-9861(61)90170-9. [DOI] [PubMed] [Google Scholar]
  5. BOOTH D. A. The isolation and assay of gangliosides and their interactions with basic proteins. J Neurochem. 1962 May-Jun;9:265–276. doi: 10.1111/j.1471-4159.1962.tb09448.x. [DOI] [PubMed] [Google Scholar]
  6. CALLANAN M. J., CARROLL W. R., MITCHELL E. R. Physical and chemical properties of protamine from the sperm of salmon (Oncorhynchus tschawytscha). J Biol Chem. 1957 Nov;229(1):279–287. [PubMed] [Google Scholar]
  7. CARROLL W. R., CALLANAN M. J., SAROFF H. A. Physical and chemical properties of protamine from the sperm of salmon (Oncorhynchus tschawytscha). II. Anion binding characteristics. J Biol Chem. 1959 Sep;234:2314–2316. [PubMed] [Google Scholar]
  8. 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]
  9. EMANUEL C. F., CHAIKOFF I. L. An hydraulic homogenizer for the controlled release of cellular components from various tissues. Biochim Biophys Acta. 1957 May;24(2):254–261. doi: 10.1016/0006-3002(57)90191-9. [DOI] [PubMed] [Google Scholar]
  10. GIBSON K. D., WILSON J. D., UDENFRIEND S. The enzymatic conversion of phospholipid ethanolamine to phospholipid choline in rat liver. J Biol Chem. 1961 Mar;236:673–679. [PubMed] [Google Scholar]
  11. 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]
  12. GREEN I., MOMMAERTS W. F. Adenosinetriphosphatase systems of muscle. IV. Kinetics of myosin adenosinetriphosphatase. J Biol Chem. 1954 Oct;210(2):695–702. [PubMed] [Google Scholar]
  13. HANZON V., TOSCHI G. Centrifugation of brain microsomes in a density gradient. Exp Cell Res. 1960 Nov;21:332–346. doi: 10.1016/0014-4827(60)90265-2. [DOI] [PubMed] [Google Scholar]
  14. HELE P., FINCH L. R. Amino acid-activating systems from pig liver. Biochem J. 1960 May;75:352–363. doi: 10.1042/bj0750352. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. JARNEFELT J. The relative rates of adenosinetriphosphatase and phosphatidic acid synthesis in microsomes from rat brain. Exp Cell Res. 1961 Oct;25:211–213. doi: 10.1016/0014-4827(61)90329-9. [DOI] [PubMed] [Google Scholar]
  16. KOSHLAND D. E., Jr The active site and enzyme action. Adv Enzymol Relat Subj Biochem. 1960;22:45–97. doi: 10.1002/9780470122679.ch2. [DOI] [PubMed] [Google Scholar]
  17. KUBO S., TOKURA S., TONOMURA Y. On the active site of myosin A-adenosine triphosphatase. I. Reaction of the enzyme with trinitrobenzenesulfonate. J Biol Chem. 1960 Oct;235:2835–2839. [PubMed] [Google Scholar]
  18. LITTLEFIELD J. W., KELLER E. B., GROSS J., ZAMECNIK P. C. Studies on cytoplasmic ribonucleoprotein particles from the liver of the rat. J Biol Chem. 1955 Nov;217(1):111–123. [PubMed] [Google Scholar]
  19. LOWENSTEIN J. M. The stimulation of transphosphorylation by alkali-metal ions. Biochem J. 1960 May;75:269–274. doi: 10.1042/bj0750269. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. LOWRY O. H., ROBERTS N. R., WU M. L., HIXON W. S., CRAWFORD E. J. The quantitative histochemistry of brain. II. Enzyme measurements. J Biol Chem. 1954 Mar;207(1):19–37. [PubMed] [Google Scholar]
  21. 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]
  22. MCILWAIN H. Characterization of naturally occurring materials which restore excitability to isolated cerebral tissues. Biochem J. 1961 Jan;78:24–32. doi: 10.1042/bj0780024. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. McIlwain H. Protein interactions and metabolic response to stimulating agents in isolated cerebral tissues: histones as inhibitors. Biochem J. 1959 Nov;73(3):514–521. doi: 10.1042/bj0730514. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. McIlwain H., Woodman R. J., Cummins J. T. Basic proteins and the potassium movements and phosphates of cerebral tissues. Biochem J. 1961 Oct;81(1):79–83. doi: 10.1042/bj0810079. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. PERRY S. V., CHAPPELL J. B. The action of 2:4-dinitrophenol on myosin and mitochondrial adenosine triphosphatase systems. Biochem J. 1957 Mar;65(3):469–476. doi: 10.1042/bj0650469. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Quastel J. H., Wheatley A. H. Anaerobic oxidations. On ferricyanide as a reagent for the manometric investigation of dehydrogenase systems. Biochem J. 1938 May;32(5):936–943. doi: 10.1042/bj0320936. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. SCHWARTZ A. The effect of ouabain on potassium content, phosphoprotein metabolism and oxygen consumption of guinea pig cerebral tissue. Biochem Pharmacol. 1962 Apr-May;11:389–391. doi: 10.1016/0006-2952(62)90061-8. [DOI] [PubMed] [Google Scholar]
  28. SELA M., KATCHALSKI E. Biological properties of poly-alpha-amino acids. Adv Protein Chem. 1959;14:391–478. doi: 10.1016/s0065-3233(08)60614-2. [DOI] [PubMed] [Google Scholar]
  29. SHOWACRE J. L., DUBUY H. G. On the enzymic nature of mitochondrial characterization by Janus green B and the detection of Krebs-cycle dehydrogenases with Janus green B. J Natl Cancer Inst. 1955 Aug;16(1):173–194. [PubMed] [Google Scholar]
  30. SKOU J. C. The influence of some cations on an adenosine triphosphatase from peripheral nerves. Biochim Biophys Acta. 1957 Feb;23(2):394–401. doi: 10.1016/0006-3002(57)90343-8. [DOI] [PubMed] [Google Scholar]
  31. THOMSON C. G., McILWAIN H. An attachment of protamines to cerebral tissues, studied in relation to gangliosides, suramin and tissue excitability. Biochem J. 1961 May;79:342–347. doi: 10.1042/bj0790342. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. TOSCHI G. A biochemical study of brain microsomes. Exp Cell Res. 1959 Feb;16(2):232–255. doi: 10.1016/0014-4827(59)90252-6. [DOI] [PubMed] [Google Scholar]
  33. WHERRETT J. R., McILWAIN H. Gangliosides, phospholipids, protein and ribonucleic acid in subfractions of cerebral microsomal material. Biochem J. 1962 Aug;84:232–237. doi: 10.1042/bj0840232. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. 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]

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