ResearchersLinks
Pakistan Journal of ZoologyA ResearchersLinks journal
Submit manuscriptReview for this journal

Short Communication · Volume 49, Issue 6, 13 December 2017 · Open Access

Peroxidase Activity in Liver and Kidney of Labeo rohita exposed to Zinc Chloride

· ·

Affiliations & Notes ⌄
  1. 1Department of Zoology, Wildlife and Fisheries, University of Agriculture, Faisalabad 38040, Pakistan , * Corresponding author: sidraabbas2012@hotmail.com
Article Info ⌄
Journal:
Pakistan Journal of Zoology
Published:
13 December 2017
Download PDF ePub eFLIP Set Alert Get Rights Reprints

From the article

  • It was also found that peroxidase activity was significantly higher in the liver of Labeo rohita as compared to kidney under metal stress conditions.
  • The peroxidase activity was significantly increased in the liver and kidney after exposure to different concentrations of zinc chloride.

Selected from the article's own text.

Abstract

Four groups of one year old Labeo rohita were exposed to 31.37 mgL-1, 20.91 mgL-1, 7.84 mgL-1 and 6.27 mgL-1 of ZnCl2 for 30 days. The peroxidase activity was found to be significantly increased both in liver and kidney after ZnCl2 treatments. Statistically significant increase in the liver and kidney peroxidase activity of 96-h LC50 exposed fish were found as 0.621±0.004UmL-1 and 0.219±0.002UmL-1, respectively as compared to the control fish liver (0.123±0.002UmL-1) and kidney (0.056±0.004UmL-1).

Materials and methods

Fingerlings of one year old fish, Labeo rohita (6.88±0.21 g and 77.42±1.15 mm) maintained in the fish ponds of University, Fisheries Research Farms, were acclimatized to the laboratory conditions for two weeks in cemented tanks prior to the start of experiment. Fish were fed with pelleted feed twice a day. Four groups of fish, each containing ten fingerlings were exposed to 31.37±1.70 mgL-1 (96-h LC50), 20.91±1.62 mgL-1 (2/3rd of LC50), 7.84 ±1.12 mgL-1 (1/4th of LC50) and 6.27±0.95 mgL-1 (1/5th of LC50) zinc, for 30 days by using static water system with continuous aeration under laboratory conditions. Each test was conducted with three replications for each concentration/treatment and activity of peroxidase in the selected organs was compared with the control fish organs.

Fish were dissected, liver and kidney were taken out for estimation of peroxidase activity. The fish liver and kidney, after rinsing with phosphate buffer of pH 6.5 (0.2 M) to remove RBCs were homogenized in cold buffer (1:4 W/V). The homogenate was centrifuged at 10,000 rpm for 15 min at 4°C, and the supernatant was used for the determination of peroxidase activity, according to Civello et al. (1995).

The data were subjected to statistical analyses by using the Factorial experiment, with three replications for each test dose. The means for various parameters were compared by using Least Square Design test.

Results and discussion

Table I shows that statistically highly significant differences (p<0.01) existed among all the treatments as well as organs for the peroxidase activity. In both the organs viz. liver and kidney of zinc chloride stressed Labeo rohita, the peroxidase activity was found significantly (p<0.05) increased as compared to the control fish. The present findings are in conformity with the result of Saliu and Bawa-Allah (2012) who reported that the activity of peroxidase was significantly increased in the liver of zinc chloride stressed (1.120±0.62UmL-1) Clarias gariepinus as compared to the control (0.950±0.43UmL-1) fish. Similar type of results have been reported by Palaniappan and Karthikeyan (2009) for liver of Labeo rohita, by Farombi et al. (2007) for liver and kidney of Wallagu attu, and by Ikram (2014) for liver of Labeo rohita. During present research work, the peroxidase activity was found increased with an increase in metal exposure concentration that followed the order: 96-h LC50 > 2/3rd > 1/4th > 1/5th > control. Aruljothi and Samipillai (2014) also reported that peroxidase activity in the gills and brain of Labeo rohita was increased with increasing concentration of arsenic. It was also found that peroxidase activity was significantly higher in the liver of Labeo rohita as compared to kidney under metal stress conditions. The present results are in contradiction to those of Talas et al. (2008), who reported decreased activity of glutathione peroxidase in the liver tissues of Oncorhynchus mykiss (rainbow trout) after exposure of Cd+2 and Cr+3.

Conclusion

The peroxidase activity was significantly increased in the liver and kidney after exposure to different concentrations of zinc chloride. However, liver showed significantly higher enzyme activity compared to the kidney.

Acknowledgment

The authors gratefully acknowledge the support offered from the University of Agriculture, Faisalabad, Pakistan.

Statement of conflict of interest

Authors have declared no conflict of interest.

References

  1. Ahmad, I., Hamid, T., Fatima, M., Chand, H.S., Jain, S.K., Athar, M. and Raisuddin, S., 2000. Biochim. biophys. Acta, 1523: 37-48. https://doi.org/10.1016/S0304-4165(00)00098-2[CrossRef]
  2. Aruljothi, B. and Samipillai, S.S., 2014. Int. J. Mod. Res. Rev., 2: 15-19.
  3. Bahnasawy, M., Khidr, A.A. and Dheina, N., 2008. J. appl. Sci. Res., 5: 845-852.
  4. Bairoch, A., 2000. Nucl. Acids Res., 28: 304-305. https://doi.org/10.1093/nar/28.1.304[CrossRef]
  5. Boeuf, G., Bauw, G., Legrand, B. and Rambour, S., 2000. Pl. Physiol. Biochem., 38: 217-224. https://doi.org/10.1016/S0981-9428(00)00731-2[CrossRef]
  6. Cao, L., Huang, W., Liu, J., Yin, X. and Dou, S., 2010. Comp. Biochem. Physiol. C, 151: 386-392.
  7. Civello, P.M., Martinez, G.A., Chaves, A.R. and Anon, M.C., 1995. J. Agric. Fd. Chem., 43: 2596-2601. https://doi.org/10.1021/jf00058a008[CrossRef]
  8. Clegg, M.S., Hanna, L.A., Niles, B.J., Momma, T.Y. and Keen, C.L., 2005. IUBMB Life, 57: 661-669. https://doi.org/10.1080/15216540500264554[CrossRef]
  9. Davies, K.J., 1995. Biochem. Soc. Symp., 61: 1-31. https://doi.org/10.1042/bss0610001[CrossRef]
  10. Farombi, E.O., Adelowo, O.A. and Ajimoko, Y.R., 2007. Int. J. environ. Res. Publ. Hlth., 4: 158-165.
  11. Goida, C.R., Lissner, L.A., Pretto, A., da Rocha, J.B., Schetinger, M.R., Neto, J.R., Morsch, V.M. and Loro, V.L., 2007. Chemosphere, 69: 170-175. https://doi.org/10.1016/j.chemosphere.2007.04.008[CrossRef]
  12. Ikram, S., 2014. Comparative analysis of peroxidase enzyme activity in hepatic and renal tissues of cultured and wild Labeo rohita. M.Phil. thesis, Department of Zoology and Fisheries, University of Agriculture, Faisalabad, Pakistan.
  13. Kurutas, E.B., Sahan, A. and Altun, T., 2009. Turk. J. Biol., 33: 275-282.
  14. Olaifa, F.E., Olaifa, A.K., Adelaga, A.A. and Owolabi, A.G., 2004. J. biomed. Res., 7: 145-148.
  15. Oteiza, P.I., 2012. Free Radic. Biol. Med., 53: 1748-1759. https://doi.org/10.1016/j.freeradbiomed.2012.08.568[CrossRef]
  16. Oteiza, P.I. and Mackenzie, G.G., 2005. Mol. Aspects Med., 26: 245-255. https://doi.org/10.1016/j.mam.2005.07.012[CrossRef]
  17. Padi, S.S. and Chopra, K., 2002. Nephron, 92: 685-692. https://doi.org/10.1159/000064095[CrossRef]
  18. Palaniappan, P.L. and Karthikeyan, S., 2009. J. environ. Sci., 21: 229-236. https://doi.org/10.1016/S1001-0742(08)62256-1[CrossRef]
  19. Saliu, J.K. and Bawa-Allah, K.A., 2012. Resour. Environ., 2: 21-26. https://doi.org/10.5923/j.re.20120201.03[CrossRef]
  20. Sevcikova, M., Modra, H., Slaninova, A. and Svobodova, Z., 2011. Vet. Med., 56: 537-546.
  21. Talas, Z.S., Orun, I., Ozdemir, I., Erdogan, K., Alkan, A. and Yilmaz, I., 2008. Fish Physiol. Biochem., 34: 217-222. https://doi.org/10.1007/s10695-007-9179-9[CrossRef]
  22. Tripathi, B.N., Mehta, S.K., Amar, A. and Gaur, J.P., 2006. Chemosphere, 62: 538-544. https://doi.org/10.1016/j.chemosphere.2005.06.031[CrossRef]
  23. Vesey, D.A., 2010. Toxicol. Lett., 198: 13-19. https://doi.org/10.1016/j.toxlet.2010.05.004[CrossRef]

Related articles

Services

Article usage statistics

Loading…

Peroxidase Activity in Liver and Kidney of Labeo rohita exposed to Zinc Chloride · ResearchersLinks