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Histochemistry

, Volume 46, Issue 1, pp 77–80 | Cite as

Localizing acethyl-serotonin transferase by electron microscopy

  • N. A. Kerényi
  • P. Sótonyi
  • E. Somogyi
Article

Summary

N-acethylserotonin, the substrate of hydroxy-indol-o-methyl-transferase (HIOMT) is being synthetized by the serotonin-acethyl-transferase. The localization of the enzyme in the pineal gland has been studied by uranyl and copper ferrocyanide methods. Both methods revealed a mitochondrial localization. The reaction precipitate was situated on the outer and inner membrane as well as in the inner compartment of the mitochondrium. Without acethyl-Co A the reaction failed to take place. Copper ferrocyanide was found more favourable than the uranyl ferrocyanide. No specific reaction, extramitochondrial precipitate occured.

Keywords

Melatonin Pineal Gland Ferrocyanide Potassium Ferricyanide Mitochondrial Localization 
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.

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References

  1. Axelrod, J., Lerner, A. B.: O methylation in the conversion of tyrosine to melanin. Biochem. biophys. Acta (Amst.)71, 650–655 (1963)CrossRefGoogle Scholar
  2. Axelrod, J., Weisbach, H.: Ourification and properties of hydroxyindol-O-methyl transferase. J. biol. Chem.236, 211–213 (1961)PubMedGoogle Scholar
  3. Axelrod, J., Weisbach, H.: Enzymatic O-methylation of N-acethylserotonin to melatonin. Science131, 1312 (1960)PubMedGoogle Scholar
  4. Barchas, J. D., Lerner, A. B.: Localization of melatonin in the nervous system. J. Neurochem.2, 489–491 (1964)Google Scholar
  5. Boadle, M. C., Bloom, F. E.: A method for the structural demonstration of monoamine oxidase activity. III. Internat. Congr. Histochem. Cytochem. New York, p. 22 (1968)Google Scholar
  6. Boadle, M. C., Bloom, F. E.: A method for the fine structural localization of monoamine oxidase. J. Histochem. Cytochem.17, 331–340 (1969)PubMedGoogle Scholar
  7. Glenner, G. G., Burther, H. G., Brown, G. W.: The histochemical demonstration of monoamine oxidase activity by tetrasolium salts. J. Histochem. Cytochem.5, 591–600 (1957)PubMedGoogle Scholar
  8. Lerner, A. B., Case, J. D., Takahashi, Y., Lee, T. H., Mori, W.: Isolation of melatonin the pineal gland factor that lightens melanocytes. J. Amer. chem. Soc.80, 2578 (1958)CrossRefGoogle Scholar
  9. Lerner, A. B., Case, J. D., Takahashi, Y.: Isolation of melatonin and 5-methoxyindole-3-acetic acid. J. biol. Chem.235, 2043–2049 (1960)Google Scholar
  10. Robertis, E. de, Pellegrino, de Iraldi, A.: Plurivesicular secretory progresses and nerve sendings in the pineal gland of the rat. J. biophys. biochem. Cytol.10, 361–362 (1961)CrossRefGoogle Scholar
  11. Wolfe, D. E., Potter, L. T., Richardson, K. C., Axelrod, J.: Localizing tritiated norepinephrine in sympathetic axons by electron microscopic autoradiography. Science138, 440–442 (1962)PubMedGoogle Scholar
  12. Wurtman, R. J., Axelrod, J., Philips, L. S.: Melatonin synthesis in the pineal gland: Control by light. Science142, 1071–1073 (1963)PubMedGoogle Scholar

Copyright information

© Springer-Verlag 1975

Authors and Affiliations

  • N. A. Kerényi
    • 1
    • 2
  • P. Sótonyi
    • 1
    • 2
  • E. Somogyi
    • 1
    • 2
  1. 1.Department of PathologySunnybrook HospitalTorontoCanada
  2. 2.Institute of Forensic MedicineSemmelweis University, Medical SchoolBudapest

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