, Volume 44, Issue 4, pp 307–312 | Cite as

Fine structural localization of arylsulfatase B activity in the rabbit blood platelets

  • Fusayoshi Murata
  • Tetsuji Nagata
  • Samuel S. Spicer


Fine structural localization of arylsulfatase in the rabbit blood platelets has been investigated in this study. Among many cell organellae, reaction products were exclusively observed in the alpha granules of the platelets. Whithin the alpha granules, arylsulfatase activity appeared to localize in variable patterns, i.e. reaction products confined mainly at the peripheral region in many granules, while they deposited heavily throughout the granule matrices in some others. In a blood platelets, each alpha granule showed the different staining pattern which indicated more variable functional heterogeneity in the granules.


Public Health Structural Localization Staining Pattern Variable Pattern Peripheral Region 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Austin, J.H., Bischel, M.A.: Histochemical method for sulfatase activity in hemic cells and organ imprints. Blood 17, 212–214 (1961)Google Scholar
  2. Bainton, D.F., Farquhar, M.G.: Differences in enzyme content of azurophil and specific granules of polymorphonuclear leukocytes. II. Cytochemistry and electron microscopy of the bone marrow cells. J. Cell Biol. 39, 299–317 (1968)Google Scholar
  3. Bainton, D.F., Farquhar, M.G.: Segregation and packaging of granule enzymes in eosinophilic leukocytes. J. Cell Biol. 45, 54–73 (1970)Google Scholar
  4. Bak, I.J., May, B., Hasler, R.: Electron microscopical demonstration of acid phosphatase in blood platelets. Z. Zellforsch. 96, 641–648 (1969)Google Scholar
  5. Beck, F., Llyod, J.B.: Lysosomes in biology and pathology. Histochemistry and electron microscopy of lysosomes, vol. 2. p. 567–599. Amsterdam: North Holland Publ. 1969Google Scholar
  6. Day, H.J., Holmsen, H., Hovig, T.: Subcellular particles of human platelets. Scand. J. Haematol. Suppl. No. 7, 1–35 (1968)Google Scholar
  7. de Duve, C.: General properties of lysosomes. The lysosome concept. Ciba Foundation Symposium: lysosome (Reuck, A.V.S. and Cameron, M.P. eds.), p. 1–35, Boston, Mass., Little, Brown and Company 1963Google Scholar
  8. Goldfischer, S.: The cytochemical demonstration of lysosomal arylsulfatase activity by light and electron microscopy. J. Histochem. Cytochem. 13, 520–523 (1965)Google Scholar
  9. Hopus-Havu, V.K., Arstila, A.U., Helminen, H.J., Kalimo, H.O., Glenner, G.G.: Improvements in the method for the electron microscopic localization of aryl-sulphatase activity. Histochemie 8, 54–64 (1967)Google Scholar
  10. Ide, H., Fishman, W.H.: Dual localization of β-glucuronidase and acid phosphatase in lysosomes and microsomes. II. membrane associated enzymes. Histochemie 20, 300–321 (1969)Google Scholar
  11. Luft, J.H.: Improvements in epoxy resin embedding method. J. biophys. biochem. Cytol. 9, 409–414 (1961)Google Scholar
  12. Makita, T., Sandborn, F.B.: Ultrastructural localization of arylsulfatase B in mitochondria of epithelial cells of the proximal convoluted tubules of the rat kidney. Experientia (Basel) 27, 187–189 (1971)Google Scholar
  13. Marcus, A.J., Zucker-Franklin, D., Safier, L.B., Ullman, H.L.: Studies on human platelet granules and membrane. J. clin. Invest. 45, 14–28 (1966)Google Scholar
  14. Murata, F., Spicer, S.S.: Morphological and cytochemical studies of rabbit heterophilic leukocytes: evidence for tertiary granules. Lab. Invest. 29, 65–72 (1973a)Google Scholar
  15. Murata, F., Hardin, J.H., Spicer, S.S.: Coexistence of acid phosphatase and acid mucosubstance in the nucleoid of human blood platelet granules. Histochemie. 35, 319–329 (1973b)Google Scholar
  16. Nicholas, B.A., Bainton, D.F., Farquhar, M.G.: Differentiation of monocytes: origin, nature, and fate of their azurophil granules. J. Cell Biol. 50, 498–515 (1971)Google Scholar
  17. Polásěk, J., Rotrekl, B.: Aryl sulphatases of human blood platelets. Nature (Lond.) 214, 187–188 (1967)Google Scholar
  18. Sabatini, D.D., Bensch, K., Barrnett, R.J.: Cytochemistry and electron microscopy: the preservation of cellular ultrastructure and enzymatic activity by aldehyde fixation. J. Cell Biol. 17, 19–58 (1963)Google Scholar
  19. Seljelid, R., Helminen, H.J.: The localization of arylsulfatase activity in thyroid follicle cells. J. Histochem. Cytochem. 16, 407–412 (1968)Google Scholar
  20. Siegel, A., Lüscher, E.F.: Non-identity of the α granules of human blood platelets with typical lysosomes. Nature (Lond.) 215, 745–747 (1967)Google Scholar
  21. Smutka, P., Brunning, R.D.: An evaluation of nuclear arylsulfatase activity in acute leukemias. Acta haemat. (Basel) 41, 290–295 (1969)Google Scholar
  22. Thyberg, J.: Ultrastructural localization of arylsulfatase activity in the epiphyseal plate. J. Ultrastruct. Res. 38, 332–342 (1972)Google Scholar

Copyright information

© Springer-Verlag 1975

Authors and Affiliations

  • Fusayoshi Murata
    • 1
    • 2
  • Tetsuji Nagata
    • 1
    • 2
  • Samuel S. Spicer
    • 1
    • 2
  1. 1.Department of AnatomyShinshu University School of MedicineMatsumotoJapan
  2. 2.Department of PathologyMedical University of South CarolinaCharlestonUSA

Personalised recommendations