Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1963 May 1;17(2):279–288. doi: 10.1083/jcb.17.2.279

THE FINE LOCALIZATION OF NUCLEOSIDE TRIPHOSPHATASE ACTIVITY IN THE RETINA OF THE FROG

Dante G Scarpelli 1, Elson L Craig 1
PMCID: PMC2106202  PMID: 13976534

Abstract

Nucleoside triphosphatase (NTPase) activity was demonstrated at the submicroscopic level in the frog retina by the Wachstein-Meisel method utilizing various purine and pyrimidine nucleosides. Under the electron microscope magnesium-activated NTPase was localized in the outer and inner segments, and in the plexiform layers. NTPase active sites in the cones were localized diffusely in the 70 to 80 A interspaces between the double membranes of the stacked lamellae and in the investing cytoplasm. In the rods, on the other hand, sites of activity were observed at the periphery of the stacked lamellae as discrete electron opaque deposits measuring 1000 to 1500 A which interdigitated between the lamellae for short distances. Deposits of reaction product appeared more numerous in rods of dark-adapted frogs stimulated with monochromatic light with a wave length of 510 mµ. Enzyme activity was also observed in mitochondria of the rod and cone ellipsoids. In the outer and inner plexiform layers NTPase active sites were present on and between the membranes of axons and the plasma membranes of some of the neurons.

Full Text

The Full Text of this article is available as a PDF (1.1 MB).

Selected References

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

  1. ABOOD L. G., GERARD R. W. Enzyme distribution in isolated particulates of rat peripheral nerve. J Cell Physiol. 1954 Jun;43(3):379–392. doi: 10.1002/jcp.1030430310. [DOI] [PubMed] [Google Scholar]
  2. COOPER C., LEHNINGER A. L. Oxidative phosphorylation by an enzyme complex from extracts of mitochondria. IV. Adenosinetriphosphatase activity. J Biol Chem. 1957 Jan;224(1):547–560. [PubMed] [Google Scholar]
  3. CRAIG E. L., FRAJOLA W. J., GREIDER M. H. An embedding technique for electron microscopy using EPON 812. J Cell Biol. 1962 Jan;12:190–194. doi: 10.1083/jcb.12.1.190. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. DE BERARDINIS E., AURICCHIO G. Sull'attivita adenilpirofosfatasica della retina. Boll Soc Ital Biol Sper. 1951 Jan-Feb;27(1-2):68–71. [PubMed] [Google Scholar]
  5. ERNSTER L., LINDBERG O. Animal mitochondria. Annu Rev Physiol. 1958;20:13–42. doi: 10.1146/annurev.ph.20.030158.000305. [DOI] [PubMed] [Google Scholar]
  6. ESSNER E., NOVIKOFF A. B., MASEK B. Adenosinetriphosphatase and 5-nucleotidase activities in the plasma membrane of liver cells as revealed by electron microscopy. J Biophys Biochem Cytol. 1958 Nov 25;4(6):711–716. doi: 10.1083/jcb.4.6.711. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. GERGELY J. Studies on myosin-adenosinetriphosphatase. J Biol Chem. 1953 Feb;200(2):543–550. [PubMed] [Google Scholar]
  8. GORNALL A. G., BARDAWILL C. J., DAVID M. M. Determination of serum proteins by means of the biuret reaction. J Biol Chem. 1949 Feb;177(2):751–766. [PubMed] [Google Scholar]
  9. KIELLEY W. W., KALCKAR H. M., BRADLEY L. B. The hydrolysis of purine and pyrimidine nucleoside triphosphates by myosin. J Biol Chem. 1956 Mar;219(1):95–101. [PubMed] [Google Scholar]
  10. NOVIKOFF A. B., HAUSMAN D. H., PODBER E. The localization of adenosine triphosphatase in liver: in situ staining and cell fractionation studies. J Histochem Cytochem. 1958 Jan;6(1):61–71. doi: 10.1177/6.1.61. [DOI] [PubMed] [Google Scholar]
  11. NOVIKOFF A. B., HECHT L., PODBER E., RYAN J. Phosphatases of rat liver. I. The dephosphorylation of adenosinetriphosphate. J Biol Chem. 1952 Jan;194(1):153–170. [PubMed] [Google Scholar]
  12. PADYKULA H. A., HERMAN E. The specificity of the histochemical method for adenosine triphosphatase. J Histochem Cytochem. 1955 May;3(3):170–195. doi: 10.1177/3.3.170. [DOI] [PubMed] [Google Scholar]
  13. PERSIJN J. P., DAEMS W. T., de MAN J., MEIJER A. E. The demonstration of adenosinetriphosphatase activity with the electronmicroscope. Z Zellforch Microsk Anat Histochem. 1961;2:372–382. doi: 10.1007/BF00848042. [DOI] [PubMed] [Google Scholar]
  14. PLAUT G. W. An inosinediphosphatase from mammalian liver. J Biol Chem. 1955 Nov;217(1):235–245. [PubMed] [Google Scholar]
  15. SCARPELLI D. G., PEARSE A. G. Physical and chemical protection of cell constituents and the precise localization of enzymes. J Histochem Cytochem. 1958 Sep;6(5):369–376. doi: 10.1177/6.5.369. [DOI] [PubMed] [Google Scholar]
  16. SPATER H. W., NOVIKOFF A. B., MASEK B. Adenosinetriphosphatase activity in the cell membranes of kidney tubule cells. J Biophys Biochem Cytol. 1958 Nov 25;4(6):765–770. doi: 10.1083/jcb.4.6.765. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. WACHSTEIN M., LANGE K. Histologic and histochemical studies of the rabbit glomerulonephritis produced by specific antikidney duck serum. Am J Pathol. 1958 Sep-Oct;34(5):835–861. [PMC free article] [PubMed] [Google Scholar]
  18. WACHSTEIN M., MEISEL E. Histochemistry of hepatic phosphatases of a physiologic pH; with special reference to the demonstration of bile canaliculi. Am J Clin Pathol. 1957 Jan;27(1):13–23. doi: 10.1093/ajcp/27.1.13. [DOI] [PubMed] [Google Scholar]
  19. WALD G., BROWN P. K., SMITH P. H. Iodopsin. J Gen Physiol. 1955 May 20;38(5):623–681. doi: 10.1085/jgp.38.5.623. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES