Species-specific differences in the substrate-inhibitory specificity of cholinesterases from optical ganglia of squids of the Gonatidae family

  • E. V. Rozengart
  • N. E. Basova
Comparative and Ontogenic Biochemistry


A comparative study was carried out of the substrate and inhibitory specificity of cholinesterase preparations from squids, representatives of 3 genes and 5 species of the Gonatidae family:Berryteuthis (B. magister andB. anonichos),Gonatus (G. kamtschaticus andG. tinro), andGonatipsis (G. borealis), that have overlapping habitation areals in the Bering Sea. As substrates, there were used bromides of acetylthiocholine, propionylthiocholine, and butyrylthiocholine, as organophosphorus inhibitors, diisopropylfluorophosphate, a cation-containing inhibitor, and 4 hydrophobic compounds. The homogeneity of the cholinesterase activity in these preparations has been shown, the intergenus and interspecies differences in the enzyme properties are revealed, and also the peculiarity of properties of enzymes from Gonatidae squids is emphasized in comparison with cholinesterase from the Pacific squidTodarodes paciflcus and “standard” mammalian enzymes (from human erythrocytes and horse blood serum). The revealed interspecies differences are discussed in terms of evolutionary development of the Gonatidae family.


Cholinesterase Evolutionary Biochemistry Optical Ganglion Butyrylthiocholine Horse Blood Serum 
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. 1.
    Rozengart, E.V., Inhibitory Specificity of Cholinesterase from Squid Optical Ganglia. Anticholinesterase Efficiency of O-ethyl-n-alkylmethylthiophosphonates,Reakts. Sposob. Org. Soed., 1967, vol. 4, pp. 954–962.Google Scholar
  2. 2.
    Turpaev, T.M., Brestkin A.P., Rosengart, E.V.,et al., Cholinesterase of Squid Optical Ganglia,Eur. J. Biochem., 1968, vol. 6, pp. 55–59.PubMedCrossRefGoogle Scholar
  3. 3.
    Nesis, K.N.,Okeanicheskie golovonogie mollyuski (Oceanic Cephalopod Molluscs), Moscow, 1985.Google Scholar
  4. 4.
    Brestkin, A.P., Kuznetsova, L.P., Moralev, S.N.,et al.,Kholinesterazy nazemnykh zhivotnykh i gidrobiontov (Cholinesterases of Terrestrial Animals and Hydrobionts), Vladivostok, 1997.Google Scholar
  5. 5.
    Rozengart, E.V., Basova, N.E., Khovanskikh, A.E., and Epshtein, L.M., Various Aspects of Substrate Specificity of Cholinesterase from Optical Ganglia of the Pacific SquidTodarodes pacifiais, Zh. Evol. Biokhim. Fiziol., 1996, vol. 32, pp. 384–392.PubMedGoogle Scholar
  6. 6.
    Rozengart, E.V., Khovanskikh, A.E., and Epshtein, L.M., Peculiarities of Inhibitory Specificity of Cholinesterase of the Pacific SquidTodarodes pacifiais, Zh. Evol. Biokhim. Fiziol., 1993, vol. 29, pp. 475–481.Google Scholar
  7. 7.
    Rozengart, E.V., Reactivity of Cholinesterase of the Commodore SquidBerryteuthis magister. Substrates and Organophosphorus Inhibitors,Zh. Evol. Biokhim. Fiziol., 1996, vol. 32, pp. 576–583.PubMedGoogle Scholar
  8. 8.
    Rozengart, E.V., Basova, N.E., Khovanskikh, A.E.,et al., Interaction of Cholinesterase of Commodore SquidBerryteuthis magister Individuals from Different Zones of the Habitation Areal with Onium Reversible Inhibitors,Zh. Evol. Biokhim. Fiziol., 1997, vol. 33, pp. 371–382.Google Scholar
  9. ba]9.
    Epshtein, L.M., Shevtsova, S.P., Rozengart, E.V.,et al., A Method for Determination of the Species Specificity of Aquatic Organisms, USSR Inventor’s Certificate no. 1001898 from 09.11.1982,Byull. Izobret., 1983, no. 9 from 07.03.1983.Google Scholar
  10. 10.
    Rozengart, E.V., Derzhavin, D.K., Kovalev, N.N.,et al., Specific Differences in Substrate Specificity of Cholinesterases of Far East Squids of the Gonatidae Family,Doklady RAN, 1995, vol. 342, pp. 703–704.Google Scholar
  11. 11.
    Epshtein, L.M., Comparative Studies of Serine Hydrolases in Hydrobionts,Doctorate Sci. Diss., St. Petersburg, 1992.Google Scholar
  12. 12.
    Ellman, G.H., Courtney, R.D., Andres, V., and Featherstone, K.M., A New and Rapid Colorimetric Determination of Acetylcholinesterase Activity,Biochem. Pharmacol., 1961, vol. 7, pp. 88–95.PubMedCrossRefGoogle Scholar
  13. 13.
    Rozengart, E.V., Khovanskikh, A.E., and Epshtein, L.M., Study of Homogeneity of Cholinesterases in the Nervous Tissue of Squids by a Method of the Substrate-Inhibitor Analysis,Zh. Evol. Biokhim. Fiziol., 1994, vol. 30, pp. 15–22.Google Scholar
  14. 14.
    Grigor’eva, G.M., Rozengart, E.V., and Turpaev, T.M., Characteristics of Specificity of Cholinesterases in the Heart and Hemolymph of Molluscs,Fiziologiya i biokhimiya bespozvonochnykh (Physiology and Biochemistry of Invertebrates), Kreps, E.M., Ed., Leningrad, 1968, pp. 166–175.Google Scholar

Copyright information

© MAIK “Nauka/Interperiodica” 2000

Authors and Affiliations

  • E. V. Rozengart
    • 1
  • N. E. Basova
    • 1
  1. 1.Sechenov Institute of Evolutionary Physiology and BiochemistryRussian Academy of SciencesSt. PetersburgRussia

Personalised recommendations