Comparative study of substrate and inhibitory specificity of monoamine oxidase of squid optic ganglia

  • O. V. Yagodina
Comparative and Ontogenic Biochemistry


Comparative study of substrate specificity of monoamine oxidase (MAO) of optic ganglia of the Pacific squid Todarodes pacificus and the Commander squid Berryteuthis magister has been carried out. The enzyme of the Pacific squid, unlike that of the Commander squid, has been established to be able to deaminate not only tyramine, tryptamine, serotonin, benzylamine, and β-phenylethylamine, but also histamine-substrate of diamine oxidase (DAO). In relation to all studied substrates, the MAO activity of optic ganglia of T. pacificus is several times higher as compared with that of B. magister. In the case of deamination of serotonin this difference was the highest and amounted to 5 times. Semicarbazide, the classic DAO inhibitor, at a concentration of 10 mM did not inhibit catalytic activity of both studied enzymes. The substrate-inhibitory analysis with use of deprenyl and clorgyline, specific inhibitors of different MAO forms, indicates homogeneity of the enzyme of the Pacific squid and heterogeneity of the Commander squid enzyme whose composition seems to contain at least two MAO forms. There are obtained quantitative differences in substrate specificity and reaction capability with respect to the inhibitors clorgylin and deprenyl for MAO of optic ganglia of the studied squid species. These differences probably can be explained by significant differences in the evolutionary level of these biological species.

Key words

evolution monoamine oxidase monoamines squids 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Gorkin, V.Z., Aminooksidazy i ikh znachenie v meditsine (Aminoxidases and Their Significance in Medicine), Moscow, 1981.Google Scholar
  2. 2.
    Nesis, K.N., Okeanicheskie golovonogie mollyuski. Rasprostranenie, zhisnennye formy, evolyutsiya (Oceanic Cephalopod Molluscs. Distribution, Life Forms, Evolution), Moscow, 1985.Google Scholar
  3. 3.
    Brestkin, A.P., Kuznetsova, L.P., Moralev, S.N., Rozengart, E.V., and Epshtein, L.M., Kholinesterazy nazemnykh zhivotnykh i gidrobiontov (Cholinesterases of Terrestrial Animals and Hydrobionts), Vladivostok, 1997.Google Scholar
  4. 4.
    Blaschko, H. and Hawkins, J., Observations on Amine Oxidase in Cephalopods, J. Physiol. (London), 1952, vol. 118, pp. 88–93.Google Scholar
  5. 5.
    Blaschko, H. and Hope, D.B., Observations on the Distribution of Amine Oxidase in Invertebrates, Arch. Biochem., 1957, vol. 69, pp. 10–15.CrossRefPubMedGoogle Scholar
  6. 6.
    Blaschko, H., The Natural History of Amine Oxidases, Rev. Physiol. Biochem. Pharmacol., 1974, vol. 70, pp. 83–148.CrossRefPubMedGoogle Scholar
  7. 7.
    Bertaccini, G., Discussion Remark, Regional Neurochemistry, Kety, S.S. and Elkes, J., Eds., Oxford; London; New York; Paris, 1961, pp. 305–306.Google Scholar
  8. 8.
    Boadle, M.C., Observations on Histaminase of Invertebrate Origin: a Contribution to the Study of Cephalopod Amine Oxidases, Comp. Biochem. Physiol., 1969, vol. 30, pp. 611–620.CrossRefPubMedGoogle Scholar
  9. 9.
    Blaschko, H. and Himms, J.M., Enzymic Oxidation in Decapods, J. Exp. Biol., 1954, vol. 31, pp. 1–7.Google Scholar
  10. 10.
    Youdim, M.B.H., Feldman, S.C., Pappas, G.D., and Pollard, H.B., Serotonin Metabolism and the Nature of Monoamine Oxidase in Squid Central Nervous System, Brain Res., 1986, vol. 381, pp. 300–304.CrossRefPubMedGoogle Scholar
  11. 11.
    Antipov, A.D., Kostkin, V.B., Rozengart, E.V., and Epshtein, L.M., Comparative Analysis of Activity of Monoamine Oxidase in Tissues of the Abyssal Squid and the Mouse under Conditions of Normal and a Increased Pressure of Environment, Zh. Evol. Biokhim. Fiziol., 1996, vol. 32, pp. 233–239.PubMedGoogle Scholar
  12. 12.
    Severina, I.S., About the Possible Mechanism of Selective Inhibition by Clorgylin and Deprenyl of Activity of Liver Mitochondrial Monoamine Oxidase of Rats, Biokhimiya, 1979, vol. 44, pp. 195–204.Google Scholar
  13. 13.
    Cornish-Bowden, E., Osnovy fermentativnoi kinetiki (Grounds of Enzymatic Kinetics), Moscow, 1979.Google Scholar
  14. 14.
    Rozengart, E.V., Reactivity of Cholinesterases of Commander Squid Berryteuthis magister. Substrates and Organophosphorus Inhibitors, Zh. Evol. Biokhim. Fiziol., 1996, vol. 32, pp. 576–583.PubMedGoogle Scholar
  15. 15.
    Yagodina, O.V. and Basova, N.E., Comparative Study of Catalytic Properties of Monoamine Oxidase of Liver of Squid Todarodes pacificus and of Liver of Wistar Rat, Zh. Evol. Biokhim. Fiziol., 2001, vol. 37, pp. 175–179.Google Scholar
  16. 16.
    Yagodina, O.V., Catalytic Property of Monoamine Oxidases in Liver of Commander Squid Berryteuthis magister from Different Regions of Habitation, Zh. Evol. Biokhim. Fiziol., 2009, vol. 45, pp. 385–390.Google Scholar
  17. 17.
    Moralev, S.N. and Rozengart, E.V., Comparative Enzymology of Cholinesterases, Intern. Univ. Lines, Biotechnology Series, no. 6, La Jolla (CA), 2007.Google Scholar
  18. 18.
    Shatemirova, K.K., Verevkina, I.V., and Gorkin, V.Z., About Inhibition Activities of Monoamine Oxidases of A and B Types by 2-Propyilamine Derivatives, Vopr. Med. Khim., 1977, vol. 23, no. 2, pp. 220–226.PubMedGoogle Scholar
  19. 19.
    Moskvitina, T.A., Kuchina, N.E., and Gorkin, V.Z., Kinetic Properties of Multiple Forms of Bovine Brain Monoamine Oxidase, Vopr. Med. Khim., 1982, vol. 28, no. 5, pp. 127–131.PubMedGoogle Scholar
  20. 20.
    Gorkin, V.Z., Tat’yanenko, L.V., and Moskvitina, T.A., Transformation in vitro of Monoamine Oxidase into the Enzyme Similar to Diamine Oxidase, Biokhimiya, 1968, vol. 33, pp. 393–402.Google Scholar
  21. 21.
    Nesis, K.N., Vertical Distribution of Pelagic Molluscs, Zh. Obshch. Biol., 1977, vol. 38, pp. 547–558.Google Scholar
  22. 22.
    Gorkin, V.Z., Transformation of Enzymes, Mol. Biol., 1976, vol. 10, pp. 717–735.Google Scholar

Copyright information

© Pleiades Publishing, Ltd. 2010

Authors and Affiliations

  • O. V. Yagodina
    • 1
  1. 1.Sechenov Institute of Evolutionary Physiology and BiochemistryRussian Academy of SciencesSt. PetersburgRussia

Personalised recommendations