Skip to main content
Log in

Cholinesterase activity in some species of theAllium genus

  • Original Papers
  • Published:
Biologia Plantarum

Abstract

In partly purified protein complexes obtained from 22 species of theAllium genus and 6 cultivars ofAllium cepa the activity of cholinesterases was detected and measured using the method of Ellman et al. The degree of its inhibition with 10-4 M neostigmine was also tested. It was found that the activity of cholinesterase differed in individual species up to two hundred times, while the differences in the inhibitory activity of 10-4 M neostigmine occurred only in a few cases. Individual sections and cultivars could not be characterized on the basis of the differences in the activities of the cholinesterases. Of all the sections that ofPhyllodolon shows the highest average activity. In the case of the tested cultivars distinctly the lowest activity was observed in cv. Kastická. The values of the enzymatic activity measured by Ellman’s method in this plant material include the activity of specific and unspecific cholinesterases and the part uninhibitable by neostigmine.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Bradford, M. M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. - Anal. Biochem.72: 248–254, 1976.

    Article  PubMed  CAS  Google Scholar 

  • Ellman, G. L., Courtney, K. D., Andres, V., Featherstone, R. M.: A new and rapid colorimetric determination of acetylcholinesterase activity. - Biochem. Pharmacol.7: 88–95, 1961.

    Article  PubMed  CAS  Google Scholar 

  • Ernst, M., Hartmann, E.: Biochemical characterization of an acetylcholinehydrolyzing enzyme from bean seedlings. -Plant Physiol.65: 447–450, 1980.

    PubMed  CAS  Google Scholar 

  • Fluck, R. A., Jaffé, M. J.: The acetylcholine system in plants. - Curr. Adv. Plant. Sci.5: 1–22, 1974a.

    Google Scholar 

  • Fluck, R. A., Jaffé, M. J.: The distribution of cholinesterases in plant species. - Phyto-chemistry13: 2475–2480, 1974b.

    CAS  Google Scholar 

  • Goryachenko, E. V.: [An enzyme from garlic, producing allicin (allicinase)-proteid of phospho-pyridoxal.] In Russ. - Dokl. Akad. Nauk SSSR87: 457–480, 1952.

    Google Scholar 

  • Gupta, R., Maheshwari, S. C.: Preliminary characterization of a cholinesterase from roots of Bengal gram -Cicer arietinum L. - Plant Cell Physiol.21: 1675–1679, 1980.

    CAS  Google Scholar 

  • Hadačová, V., Hofman, J., Almeida, R. M., Vackovà, K., Kutáček, M., Klozová, E.: Choline esterases and choline acetyltransferase in the seeds ofAllium altaicum (Pall.) Reyse. - Biol. Plant.23: 220–227, 1981a.

    Article  Google Scholar 

  • Hadačová, V., Klozová, E., Hadač, E., Turková, V., Pitterová, K.: Comparison of esterase isoenzyme patterns in seeds of someAllium species and in cultivars ofAllium cepa L. - Biol. Plant.23: 174–181, 1981b.

    Article  Google Scholar 

  • Kasturi, R., Vasantharajan, V. N.: Properties of acetylcholinesterase fromPisum sativum. -Phytochemistry15 : 1345–1347, 1976.

    Article  CAS  Google Scholar 

  • Klozová, E., Hadačová, V., Turková, V.: A contribution to the standardization of methods for the preparation of seed proteins ofAllium cepa L. - Biol. Plant.21: 284–290, 1979.

    Google Scholar 

  • Mansfield, D. H. G., Clark, D. G., Taylor, I. E. P.: Partial purification and some properties of a cholinesterase from bush bean (Phaseolus vulgaris L.) roots. - Biochem. J.175: 769–777, 1978.

    PubMed  CAS  Google Scholar 

  • Pearse, A. G. E.: Histochemistry, Theoretical and Applied (3. ed.). - Churchill Livingstone, Edinburgh -London 1972.

    Google Scholar 

  • Riddles, P. W., Blakeley, R. L., Zerner, B.: Ellman’s reagent 5,5′-dithiobis (2-nitrobenzoic acid) — a reexamination. - Anal. Biochem.94: 75–81, 1979.

    Article  PubMed  CAS  Google Scholar 

  • Riov, J., Jaffé, M. J.: A cholinesterase from bean roots and its inhibition by plant growth retardants. -Experientia29: 264–265, 1973a.

    Article  CAS  Google Scholar 

  • Riov, J., Jaffé, M. J.: Cholinesterase from plant tissues. I. Purification and characterization of a cholinesterase from mung bean roots. - Plant Physiol.51: 520–528, 1973b.

    Article  PubMed  CAS  Google Scholar 

  • Selby, C., Galpin, I. J., Collin, H. A.: Comparison of the onion plant (Allium cepa) and onion tissue culture. Aliinase activity and flavour precursor compounds. - New Phytol.83: 351 to 359, 1979.

    Article  Google Scholar 

  • Verheul, F. E. A. M., Draijer, J. W., Muijser, A. O., Van Gelder, B. F.: The reactivity of thiol groups in bovine heart cytochrome c oxidase towards 5,5′-dithiobis (2-nitrobenzoic acid). - Biochim. biophys. Acta681: 118, 1982.

    Article  PubMed  CAS  Google Scholar 

  • Voss, G.: Taxonomy related cholinesterase inhibition patterns in insects. - J. econ. Entomol.74 : 555–557, 1981.

    CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hadačová, V., Vacková, K., Klozová, E. et al. Cholinesterase activity in some species of theAllium genus. Biol Plant 25, 209–215 (1983). https://doi.org/10.1007/BF02902105

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02902105

Keywords

Navigation