Also, the highest activities were observed in concentration of 0.2 M NH4 2SO4 as ionic strength for both liver and brain.
📌 3 Key Takeaways
🎯
Objective & Hypothesis:In this study, acethylcholinesterase was purified from liver and brain of Van Lake fish Chalcalburnus Tarichii P.1811 by using affinity chromatography technique.
📊
Key Findings & Data:The purification folds were determined as 142 and 344 for brain and liver, respectively.
💡
Conclusion & Impact:Also, the highest activities were observed in concentration of 0.2 M NH4 2SO4 as ionic strength for both liver and brain.
In this study, acethylcholinesterase was purified from liver and brain of Van Lake fish Chalcalburnus Tarichii P.1811 by using affinity chromatography technique. The purification folds were determined as 142 and 344 for brain and liver, respectively. The purity of enzyme was controlled with sodium dodecylsulfate-polyacrylamide gel electrophoresis SDSPAGE . The optimal pH was determined as 7.5-8.5 for brain and liver, respectively. On the other hand, the optimal temperature was determined as 35oC for both liver and brain. Also, the highest activities were observed in concentration of 0.2 M NH4 2SO4 as ionic strength for both liver and brain.
AKMAN, E., TÜRKOĞLU, V., CELİK, I. (2009). Purification and Characterization of Van Lake Fish Chalcalburnus tarichii P.1811 Liver and Brain Acethylcholinesterase. Hacettepe Journal of Biology and Chemistry, Cilt: 37 - Sayı: 4, 331–336. https://ajindex.com/articles/256105
Alpuche, G.L., Gold, B.G., Determination of esterase activity and characterization of cholinesterases in the reef fish Haemulon plumieri. Ecotoxicol. Environ. Safety. 71, 787-797, 2008
Nachmansohhn, D., Chemical, molecular basis of nerve activity. Academic Press, New York, 137, 1959
Habig, C., Di Giulio, R.T., Biochemical characteristics of cholinesterase in aquatic organisms. In: Mineau, P. (Ed.), cholinesterase-inhibiting insecticides. Their impact on wildlife and the environment. Elsevier, Amsterdam, 20– 30, 1991
Nachmansohhn, D., Lededer, E., Chemical, Molecular Basis of Nevre Activity. Bull. Soc. Chim. Biol. 21, 797, 1939
Sturm, A., da Silva de Assis, H.C., Hansen, P.D., Cholinesterases of marine teleost fish: enzymological characterization and potential use in the monitoring of neurotoxic contamination. Mar. Environ. Res. 47, 389– 398, 1999 6. Varo, I., Navarro, J.C., Amat, F., Guilhermino, L., Effect of dichlorvos on cholinesterase activity of the European sea bass (Dicentrarchus labrax). Pestic. Biochem. Physiol. 75, 61–72, 2003
Rodriguez-Fuentes, G., Gold-Bouchot, G., Characterization of cholinesterase activity from different tissues of Nile tilapia (Oreochromis niloticus). Mar. Environ. Res. 58, 505–509, 2004
Monteiro, M., Quintaneiro, C., Morgado, F., Soares, A.M.V.M., Guilhermino, L., Characterization of the cholinesterases presents in head tissues of the estuarine fish Pomatoschistus microps: application to biomonitoring. Ecotoxicol. Environ. Safety. 62, 341–347, 2005
Walker, C.H., Thompson, H.M., Phylogenetic distribution of cholinesterases and related esterases. In: Mineau, P. (Ed.), Cholinesterase-inhibiting insecticides. Their impact on wildlife and the environment. Elsevier, Amsterdam, 3– 19, 1991
Brewer, G.J., Sing, C.F., An introduction to izoenzymes techniques. Academic Preaa Inc. 20, 1970
Hoz, D.L.D., Raltson, J.S., Rush, R.S., Wolfe, A.D., A Simplified procedure for the purification of large quantities of fetal bovine serum acethylcholinesterase. Life Sciences. 39, 195-199, 1986
Raltston, J.S., Rush, R.S., Doctor, P.B., Wolfe, A.D., Acethylcholinesterase from fetal bovine serum purification and characterisation of soluble G4 enzyme. J. Biol. Chem. 260, 4312-4318, 1985
Main, A.R., Soucie, W.G., Buxton, L.I., Arinc, E., The purification of cholinesterase from horse serum. The Biochem. J. 143, 733-744, 1974
Bruns, K., Casillas, E.D., Partial purification and characterization of on