M. Şirin BALA, Nurhayat ATASOY, Vedat TÜRKOĞLU

Coenuriasis Hastalıklı Koyunlarda Asetilkolinesteraz Enzimi Aktiviteleri Üzerine Bazı İlaçların İn Vitro Etkilerinin Araştırılması

B u çalışmada, sağlıklı ve halk arasında delibaş ‘’coenuriaiasis’’ olarak bilinen koyunların kan plazması ve beyin homojenatı asetilkolinesteraz enzimi aktivitelerinin karşılaştırılması yapılmış ve gerek sağlıklı ve gerek hastalıklı koyun asetilkolinesteraz enzimi üzerine bazı parazikuantal ilaçların ve geniş spektrumlu antibiyotiklerin in vitro etkileri araştırılmıştır. Hem sağlıklı hem de hastalıklı koyun enzimleri üzerine Rikobendazol, Amikasin, Gentamisin, Klindamisin ve Seftriakson ilaçlarının etkileri incelendi. Adı geçen bu ilaçlardan Rikobendazol ve Klindamisin bu enzimleri inhibe ederken Amikasin, Gentamisin ve Seftriakson ilaçlarının herhangi bir etkisinin olmadığı bulundu. Sağlıklı koyun üzerine uygulanan Rikobendazol ve Klindamisin ilaçlarının kan plazması Ideğerleri; 10.19x10-3 M ve 36.14x10-3 M olarak, hastalıklı koyun üzerine uygılanan Rikobendazol ve Klindamisin ilaçlarının kan plazması I değerleri ise 18.51x10-3 M ve 6.90x 10-2 M olarak bulundu. K değerleri sırasıyla sağlıklı koyun üzerine uygulanan Rikobendazol, Klindamisin; hastalıklı koyun üzerine uygulanan Rikobendazol, Klindamisin ilaçlar için sırasıyla 3.00x10-8 M, 7.36x10-7 M; 2.62x10-8 M ve 8.50x10-7 M olarak bulundu. Beyinde ise sağlıklı koyun üzerine uygulanan Rikobendazol ve Klindamisin ilaçlarının beyin homojenatı I50 değerleri 6.27x107 M ve 7.81x10-7 M hastalıklı koyun beyin homojenizatı I50 değerleri 27.75x10-7 M ve 7.67x10-7M olarak bulundu. Koyun beyni üzerine uygulanan Rikobendazol ve Klindamisin ilaçların Ki değerleri ise sağlıklı koyunda 3.06x10-8M ve 1.82x10-6 M olarak, hastalıklı koyunda 1.02x10-7 M ve 1.95x 10-6 M olarak bulundu. Beyin gruplarının AChE enzim aktivitelerindeki değişimin istatistiksel olarak önemli olduğu saptanmıştır p

Anahtar Kelimeler:

Asetilkolinesteraz, İnhibisyon, Plazma, Beyin, Coenuriasis Delibaş Hastalığı , Koyun

In Vitro Determination of AChE Enzyme Activity from Coenuriasis Ill Sheep to Some Drugs

In this study, the blood plasma of healthy sheep and those with ‘‘coenuriasis’’, popularly known as ‘‘gid’’ , were examined and a comparison of the activities of brain homojenizat acetylcholinesterase have been made. Lastly, a kinetic study was done. The effects of drugs such as Ricobendazole, Amikacin, Gentamicine, Clindamicine and Ceftriaxone, on both healthy and diseased sheep’s enzymes were examined. The drugs Ricobendazole and Clindamicin can inhibit the symptoms but it was observed that the other drugs had no effect. While the I50 blood plasma value of Ricobendazole and Clindamicin drugs over the healthy sheep were 10.19x10-3 M and 36.14x10-3 M, the values of these drugs over the unhealthy sheep were found as 18.51x10-3 M and 6.90x10-2 M. Further K value of Ricobendazole and Clindamicine drugs over the healthy sheep were 3.00x10-8 M and 7.36x10-7 M respectively and the same values of these drugs over the unhealthy sheep were found as 2.62x10-8 M and 8.50x10-7 M. The I50 value of Rizkobendazol and Clindamicine drugs over the healthy sheep’s brain were 6.27x10-7 M and 7.81x10-7 M, and the same values of these drugs over the unhealthy sheep’s brain were found as 27.75x10-7 and 7.67x10-7. Finally, K value of Rikobendazol and Clindamicine drugs over the healthy sheep’s brains were 3.06x10-8 M and 1.82x10-6 M and the same values of these drugs over the unhealthy sheep’s brains were found as 1.02x10-7 M and 1.95x10-6 M. Changes in the enzyme activity of brain groups was statistically significant p

Keywords:

Acetylcholinesterase, Inhibition, Plasm, Brain, Coenuriasis “gid”, Sheep,

PDF

___

1. C.H. Walker, H.M. Thompson, Phylogenetic distribution of cholinesterases and related esterases. In: Mineau, P.(Ed.), Cholinesterase-inhibiting insecticides. Their impact on wildlife and the environment. Elsevier, Amsterdam, (1991) 3.
2. H. Demir, V. Türkoğlu, Effects of neostigmine methylsulphate on enzyme activity of acetylcholinesterase in rat serum, plazma, muscle and liver in vivo. Scand. J. Lab. Anim. Sci., 32 (2005) 25.
3. I. Wilson, B. D. Nachmansohhn, In Ion Transport Across Membranes. Acedemic Pres Inc., New York. 35s, (1954).
4. D.L. Nelson, M.M. Cox, Lehninger Principles of Biochemistry. 4th Edn., WH Freeman and Company, New York, (2000).
5. C. Cristofol, G. Virkel, L.Alvarez, S. Sanchez, M. Arboix, C. Lanusse, Albendazole sulphoxide enantiomeric ratios in plasma and target tissues after intravenous administrarion of ricobendazole to cattle. J. Vet. Pharmacol. Ther., 24 (2001) 117.
6. E.A. Formentini, N. Mestorino, J.O. Errecalde, Pharmacocinetics of ricobendazole after its intravenous, intraruminal and subcutaneus administration in sheep. Vet. Res. Commun., 29 (2005) 595.
7. E.A. Formentini, O.N. Mestorino, E.L. Marino, J.O., Errecalde, Pharmacocinetics of ricobendazole in calves. J. Vet. Pharmacol. Ther., 24 (2001) 199.
8. C. Lonusse, G. Virkel, S. Sanchez, A. Alvarez, A. Lifschitz, F. Imperiale, A. Monfrinotti, Ricobendazole kinetics and availability following subcutaneous administration of a novel injectable formulation to calves. Res. Vet. Sci., 65 (1998) 5.
9. S.J. Leonard, translation: Sb Kolesnikov. Pharmacology 4. Print page No: 295
10. Anti-Infective Agents, (1998).
11. R. Moulds, M. Jeyasingham, “Gentamicin: a great way to start”. Australian Prescriber 3 (2010) 134.
12. M. Gladwin, Clinical Microbiology Made Ridiculously Simple 4th ed. Miami, FL: MedMaster (2007) Inc. p. 67.
13. F. Veronesi, E. Lepri, M.C. Marchesi, G. Fillippini, M.T. Mandara, A focus of brain coenurosis in sheep coming from an Italian umbrian stock farm. Large Anim. Rev., 14 (2008), 217.
14. A. Varcasia, G. Tosciri, G.N.S. Coccone, A.P. Pipia, G. Garippa, A. Scala, V. Damien, G. Vural, C.G. Gauci, M.W. Lightowlers, Preliminary field trial of a vaccine against coenurosis caused by Taenia multiceps. Vet. Pathol., 162 (2009) 285.
15. P.R. Scot, Diagnosis and treatment of coenurosis in sheep.Veterinary Parasitology 189 (2012) 75.
16. M.L. Doherty, H.F. Bassett, R. Breathnach, M.L. Monaghan, B.A. McLearn, Outbreak of acute coenuriasis in adult sheep in Ireland. Vet. Rec., 125 (1989) 185.
17. G.L. Ellman, K.D. Courtney, J.R.V. Andres, R.M. Featherstone, A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol., 7 (1961) 88.
18. K. Sümbüloglu, V. Sümbüloğlu, Materiality Tests. IN: Biostatistics, Sumbuloglu, K.and V. Sumbuloglu (Eds.). Hatipoglu Publisher, Ankara, (1998), pp: 76-1.
19. E. Stedman, L.H. Easson, Cholinesterase an enzyme present in the blood serum of the horse [J]. Biochem. J., (1932), pp. 121-177.
20. F. Strelitz, Studies on cholinesterase. 4. Purification of pseudocholinesterase from horse serum. Biochem. J., 38 (1944) 86.
21. A.R. Main, W.G. Soucie, L.I Buxton, E. Arinc, The purification of cholinesterase from serum. Biochem. J., 143 (1974) 733.
22. X.C. Xie, S.N. Li, G.N. Zhu, Y.J. Tan, Purification of Bra in Acetylcholinerase (AChE) from Topmouth Gudgeon and Comparative Study between Crude and Purified AChE[J]. Chinese J. Pesticide Sci., 1 (2003) 45.
23. Y. Zhang, Comparison of biochemical characteristics of acetylcholinesterase between Apis cerana cerana Fabricius and Apismellifera ligustica Spinola [D]. Fujian: Fujian Agriculture and Forestry University, (2005), pp. 71-80.
24. H. Wei, J.L. Shen, W. Wu, J.W. Zhao, Z.X. Zhan, Purification,biochemical properties and insecticidessusceptibility of acetylcholinerase from housefly(Musca domesticaL.)[J]. J. Agro-Environ. Sci., 28 (2009) 156.
25. X. Peng, Purification and characterization of acetylcholinesterase, a kind of pesticide target [D]. Sichuan: Sichuan University, (2007) 13.
26. N. Noor, Ankxiolytic action and safety of kava: Effect on rat brain acetylcholinesterase aktivity and some serum biochemicalparameters. Afri. Tournal Pharmocy Pharmacolopy, 4 ( 2010) 823.
27. F.A. Mohammad, Modified electrometric method for measurementof erythrocyte acetylcholinesterase activity in sheep. Vet Hum Toxicol. 39 (1997) 337.
28. K.A. Askar, A.C. Kdi, A.J. Moody, Comparative analysis of cholinesterase activities in food animals using modified Elman and Micheal assays. The Canad. J. Vet. Res.,75 (2011) 261.
29. Z. Soyer, S. Parlar, V. Alptüzün, Synthesis and acetylcholinesterase (AChE) inhibitory activity of some N-substituted-5-chloro-2(3H)-benzoxazolone derivatives. Marmara Pharmaceutical Journal 17 (2013) 15.
30. N. Kahraman, S. Yantural, S. Kalkan, N.C. Oray, N Hocaoğlu, A. Ugurhan, Evaluating the relationship between serum acetylcholinesterase levels and clinical course and mortality of patients presented with organophosphate and carbamate posinings. Turk. J. Emerg. Med., 8 (2008) 121.
31. E. Çapkın, Effects of carbosulfan on erythrocyte acetylcholinesterase (AChE) activities of rainbow trout (Oncorhynchus mykiss). J. Fish. Sci., 5 (2011) 240.
32. Ö.F. Güloglu, V. Türkoğlu, İ. Çelik, Purification and characterization of Acetylcholinesterase from sheep liver and ınhibition by some Poinkillers. Asian J. Chem., 13 (2006) 1097.
33. S. Guhathakurta, S. Bhattacharya, In vitro inhibition of goat brain acetylcholinesterase by pure and commercial anticholinesterase pesticides. Ecotoxicol. Environ. Safety, 17 (1989) 16.
34. N. Habila, H.M. Inuwa, I.A. Aimola, O.I Lasisi, D.G. Chechet, I.A. Okafor, Correlation of acetylcholinesterase activity in the brain and blood of wistar rats acutely infected with Trypanosoma congolense. J. Acute Dis., 1 (2012) 26.
35. D. Nachmansohn, E. Lededer, Chemical, molecular basis of nevre activity. Bull. Soc. Chim. Biol., 21 (1939) 797.
36. D. Nachmansohn, M.A. Rothenberg, Hydrolyze of the butrylcholine in the serum cholinesterase. Science, 100 (1944a) 454.
37. D. Nachmansohn, M.A. Rothenberg, Hydrolyze of the butrylcholine in the red cell enzyme. J. Biol. Chem., 158 (1944b) 653.