Effect of Ethanol on Branchial Adenosine Triphosphatases in Oreochromis mossambicus (Peters)

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  • Department of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Cochin - 682 016, Kerala ,IN
  • Department of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Cochin - 682 016, Kerala ,IN


Analysis of variance, branchial ATPases, gill, Oreochromis mossambicus


The aim of this work was to determine the toxicity of ethanol in an aquatic system by means of bioassays with Oreochromis mossambicus (Peters) as a test organism. The study revealed changes in the gill ATPase activities. The results obtained indicated that ethanol brought about a decrease in the body weight, followed by significant inhibition on total ATPase, Na+/K+ ATPase, Ca2+ ATPase and Mg2+ ATPase activities. The studies also indicated that these can be employed as suitable biomarkers in ethanol related toxicity studies.


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How to Cite

Bhanu, S. V., & Philip, B. (2018). Effect of Ethanol on Branchial Adenosine Triphosphatases in <i>Oreochromis mossambicus</i> (Peters). Toxicology International, 18(1), 27–30. Retrieved from https://www.informaticsjournals.com/index.php/toxi/article/view/21286



Original Research
Received 2018-05-18
Accepted 2018-05-18
Published 2018-05-21



Natalie LC, William GR, Brent PS, William GR. The impact of fuel ethanol on groundwater: Source behavior, 14th Annual international petroleum environmental conference, Houston, TX. Available from: http://ipec.utulsa.edu/conf 2007/ Abstracts/202007/Rixey.pdf.[Last accessed on 2007].

Bevill K. Deadly train accident continues to be investigated. Brazil: Ethanol Producer Magazine; 2009.

Peter MC, Anand SB, Peter VS. Stress tolerance in fenvalerateexposed air breathing perch: Thyroidal and ionoregulatory responses. Proc 3. India: Indian Environment Congress; 2004. p. 294-8.

Sancho E, Ferrando MD, Andreu E. Inhibition of gill Na+/ K+ ATPase activity in the eel Anguilla anguilla by fenitrothion. Ecotoxicol Environ Saf 1997;38:132-6.

Wendelaar Bonga SE. The stress response in fish. Physiol Rev 1997;77:591-625.

Kultz D, Onken H. Long-term acclimation of the teleost Oreochromis mossambicus to various salinities: Two different strategies in mastering hypertonic stress. Marine Biol 1993;117:527-33.

APHA. Standard methods for the examination of water and waste water. 20th ed. Washington, DC: American Public Health Association; 1998.

Chellan B, Ramesh M, Ramanujam RM. Lethal and sub-lethal effects of a synthetic detergent on liver, muscle and branchial Na+/K+ ATPase enzyme activity in Labeo rohita. Indian J Fish 2003;50:405-8.

Finney DJ. Probit Analysis. New York: Cambridge University Press; 1971. p. 337.

USEPA. The committee on methods for toxicity test with aquatic organisms. Methods for acute toxicity tests with fish, macro invertebrates and amphibians. Duluth Minnesota: U.S. Environ. Prot. Agency; 1975; EPA 660/3-75-009 67.

OECD. Guidance document on aquatic toxicity testing of difficult substances and mixtures. OECD Series on Testing and Assessment number 23. Paris: OECD Environment Directorate; 2000. p. 53.

Evans DH. Membrane adenosine triphosphatase of E.coli activation by calcium ions and inhibition by monovalent cations. J Bacteriol 1970;100:914-22.

Bonting SL. Sodium potassium activated adenosine triphosphatase and cat ion transport. In: Bittar EE, editor. Membrane and Ion Transport. Vol. 1. London: Interscience; 1970. p. 257-363.

Hjerten S, Pan H. Purification and characterisation of two forms of a low affinity calcium ion ATPase from erythrocyte membrane. Biochim Biophys Acta 1983;755:457-66.

Ohnishi T, Suzuki T, Ozawa K. A comparative study of plasma membrane magnesium ion ATPase activities in normal, regenerating and malignant cells. Biochim Biophys Acta 1982;684:67-74.

Fiske CH, Subba Row Y. The colorimetric determination of phosphorus. J Biol Chem 1925;66:375.

Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with folin reagent. J Biol Chem 1951;193:265-75.

Reddy AN, Venugopal NB, Reddy SL. Effect of endosulfan 35 EC on ATPases in the tissues of a freshwater field crab B. querini. Bull Environ Contam Toxicol 1992;48:216-22.

Ghate HV, Mulherkar L. Histological changes in the gills of two fresh water prawn species exposed to copper sulphite. Ind J Exp Biol 1979;17:838-40.

Preeti AK. Environment new challenges. In: G Krishnamoorthy, Sivamady, editors. Protective effect of Mucuna pruriens seed on ethanol treated rat brain ATPases. Chapter 16. India: Daya books; 2008. p. 114 -7.

Suhel P, Iqbal S, Sheikh R. Decreased gill ATPase activities in the freshwater fish Channa punctata (Bloch) exposed to a diluted paper mill effluent. Ecotoxicol Environ Saf 2006;65:62-6.

Jayantha RK, John SN. Total ATPase activity in different tissues of albino mice exposed to aluminium acetate. J Environ Biol 2007;28:483-4.

Simkiss K. Ecotoxicants at the cell-membrane barrier. In: Newman MC, Jagoe CH, editors. Boca Raton, FL: Ecotoxicology: A hierarchical treatment; 1996. p. 59-83.

Kim L, Pia K, Christian KT, Steffen SM, Frank BJ. Physiological response in the European flounder (Platichthys flesus) to variable salinity and oxygen conditions. J Comp Physiol B 2008;78: 909-15.

Ross DH, Garrett KM, Cardenas HL. The effects of Lubrol WX on brain membrane Ca2+, Mg2+ ATPase and ATP-dependent Ca2+ uptake activity following acute and chronic ethanol. Neurochem Res 1985;10:283-95.

Reddy PM, Philip GH, Bashamohideen M. Inhibition of Mg2+ and Na+/ K+ ATPases in selected tissues of fish, Cyprinus carpio under fenvalerate toxicity. Biochem Int 1991;23:715-21.

Racker E, Knowles AF, Eytan M. Resolution and reconstitution of ion-transport systems. Ann NY Acad Sci 1975;264:17-33.

Sato C, Yonei S. Membrane changes. In: CS Potten, editors. Perspectives in mammalian cell death. Oxford: Oxford University Press; 1987. p. 1-17.