Bìol. Tvarin, 2014, volume 16, issue 2, pp. 86–92


N. Nasedkina, D. Ostapiv, I. Jaremchuk, S. Kornyat

This email address is being protected from spambots. You need JavaScript enabled to view it.

Institute of animal biology NAAS,
38 V. Stusa str., Lviv 79034, Ukraine

Specific (acetylcholinesterase; AChE) and nonspecific (butyrylcholinesterase; nChE) cholinesterase activity and AChE isoform content in breeder sperm were studied. It is set, that boar sperm characterizes by low activity of AChE (16.3±1.44 nmol/min×mg protein) and nChE (6.0±0.94 nmol/min×mg protein), ram has a high values (67.7±3.21 and 25.0±2.05 nmol/min×mg protein), bull semen indicators occupy an intermediate position (AChE — 48.3±8.72 and nChE — 15.7±2.37 nmol/min×mg protein). It is found, that main part of AChE activity in breeder ejaculates falls on sperm plasma (59.5–81.6 %), and nChE — on bull and ram spermatozoa (74.8–93.6 %) and on sperm plasma — in boar (71.7 %). Bull and ram ejaculates characterizes by 5–6 main AChE isoforms and by 3–4 minor, and boar, correspondingly, 3–4 and 2–3. Quantitatively for boar ejaculates, as in plasma and bull sperm isoform content lowers with the speed migration increase of enzyme proteins in 7.5 % polyacrilamide gel. On the contrary, in bull sperm plasma and spermatozoa almost 1/3 of isoform content is AChE4 (29.3–34.1 %), lesser (10.3–18.0 %) — АChЕ3, АCЕ5 and АChЕ6 and the least is (1.9–6.6 %) АChЕ1, АChЕ2 and АChЕ7. Ram ejaculates and sperm plasma characterizes by higher content of АChЕ4 (30.9–33.1 %), lesser АChЕ5 (18.1–25.9) and the least — АChЕ7 (6.9–7.5 %). It was found that, AChE quantity and isoform content in sperm are caused by individual features, feeding and intensity of breeder usage.


  1. Doliba M. M. Cholinergic regulation of energy metabolism in the myocardium and digestive glands. Author. Thesis. Dr. biol. sci. diss. Lviv, 1993. 45 p. (in Ukrainian)
  2. Hordiy S. K., Ikkert O. V., Kurhalyuk N. M. Tkachenko H. M. ta in. Neurotransmitters and efficiency of the respiratory secretory tissues. Lviv, Publ. center of LNU named after Ivan Franko, 2006. 233 p. (in Ukrainian)
  3. Karczma A. G. Cholinesterases (ChEs) and the cholinergic system in ontogenesis and phylogenesis, and non-classical roles of cholinesterases. Chem. Biol. Interactions, 2010, vol. 187, no. 1–3, pp. 34–43. https://doi.org/10.1016/j.cbi.2010.03.009
  4. Zvereva G. V., Chuhriy B. N., Klevets L. A., Uvarova-Gogol T. Ja. Activity of acetylcholinesterase is in sperm of bulls. Doklady VASHNIL, Moscow, 1987, vol. 8, pp. 33–36. (in Russian)
  5. Nelson L. Acetylcholinesterase in bull spermatozoa. J. Reprod. Fertil., 1964, vol. 7, pp. 65–71. https://doi.org/10.1530/jrf.0.0070065
  6. Nelson L. Enzyme distribution in “naturally-decapitated” bull spermatozoa: acetylcholinesterase, adenylpyrophosphatase and adenosinetriphosphatase. J. Cell. Physiol., 1966, vol. 68, pp. 113–116. https://doi.org/10.1002/jcp.1040680205
  7. Sayko A. A. Physiological role of acetylcholine in the sperm of animals. Agricultural biology, 1969, vol. 4, no. 5, pp. 759–765. (in Russian)
  8. Nelson L., Metz C. B., Monroy A. Sperm motility in “Fertilization”. Academic Press, New York, 1967, vol. 1, pp. 27–97.
  9. Vlizlo. V. V. Laboratory research methods in biology, animal husbandry and veterinary medicine. A handbook. Lviv, Spolom, 2012, 764 p. (in Ukrainian)
  10. Lowry O. H., Rosebrough N. J., Fair A. L., Randall R. J. Protein measurement with Folin-Phenol reagents. J. Biol. Chem., 1951, vol. 193, no. 1, pp. 265–275.
  11. Karpischenko A. I. Medical laboratory technology. A handbook. Saint Petersburg, Intermedika, 2002, pp. 45–46. (in Ukrainian)
  12. Knedel M., Böttger R. Eine kinetische Methode zur Bestimmung der Aktivität der Pseudocholinesterase (Acylcholinacylhydrolase Klin Wschr., 1967, vol. 45, pp. 325–327. https://doi.org/10.1007/BF01747115
  13. Maynard E. A. Electrophoretic studies of cholinesterases in brain and muscle of the developing chicken. J. Exp. Zool., 1966, vol. 161, pp. 319–336. https://doi.org/10.1002/jez.1401610303
  14. Plohinskiy N. A. Biometrics. Moscow, MHU, 1970, p. 358. (in Russian)

Download full text in PDF format






WorldCat Logo