Sts.AcknowledgmentsFinancial help supplied by University Grants Commission-Basic Scientific Study (UGC-BSR) in the type of a single time grant towards the corresponding author is gratefully acknowledged. The instrumentation facility provided by the University Grants Commission-Special Assistance Programme (UGC-SAP) in the Department of Animal Science, Bharathidasan University, can also be acknowl-edged. The authors thank Dr. S. Pannerselvam, Professor and Head, Sugarcane10 Research Station, Sirugam-ani-Tiruchirappalli, Tamilnadu, India, for delivering the Piper betle wide variety.Evidence-Based Complementary and Option Medicine[15] Globe Overall health Organization, “FAO/WHO professional committee on food additives evaluation of specific meals additives and contaminants,” Tech. Rep. 683, WHO, Geneva, Switzerland, 1982. [16] A. M. Rimando, B. H. Han, J. H. Park, and M. C. Cantoria, “Studies on the constituents of Philippine Piper betle leaves,” Archives of Pharmacal Study, vol. 9, no. two, pp. 937, 1986. [17] A. Manigauha, S. Patel, H. Ali, A. Chandy, and M. Uma Maheshwari, “Study the impact of phytochemical constituents of Piper betle leaves extracts on liver issues by in vivo model,” Journal of Pharmacy Study, vol. two, pp. 35356, 2009. [18] P. E. Schurr, J. R. Schultz, and T. M. Parkinson, “Triton-induced hyperlipidemia in rats as an animal model for screening hypolipidemic drugs,” Lipids, vol. 7, no. 1, pp. 684, 1972. [19] M. M. Bradford, “A rapid and sensitive technique for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding,” Analytical Biochemistry, vol. 72, no. 1-2, pp. 24854, 1976. [20] T. Sasaki, S. Matzy, as well as a. Sonal, “Effect of acetic acid concentration around the colour reaction in the O-toluidine boric acid process for blood glucose estimation,” Rinsho Kagaku, vol. 1, pp. 34653, 1972. [21] W. T. Friedewald, R. I. Levy, and D. S. Fredrickson, “Estimation on the concentration of low-density lipoprotein cholesterol in plasma, with no use of the preparative ultracentrifuge,” Clinical Chemistry, vol. 18, no. six, pp. 49902, 1972. [22] J.Azidoacetic Acid Technical Information King, “The transferases-alanine and aspartate transaminases,” in Practical Clinical Enzymology, D. Van, Ed., pp. 12138, D. Van Nostrand, London, UK, 1965. [23] J. King, “The hydrolases-acid and alkaline phosphatases,” in Sensible Clinical Enzymology, D. Van, Ed., pp. 19108, D. Van Nostrand, London, UK, 1965. [24] J. King, “The dehydrogenases or oxidoreductases lactate dehydrogenase,” in Practical Clinical Enzymology, D. Van, Ed., D. Van Nostrand, London, UK, 1965. [25] A. K. Sinha, “Colorimetric assay of catalase,” Analytical Biochemistry, vol. 47, no. two, pp. 38994, 1972. [26] S. Marklund and G. Marklund, “Involvement on the superoxide anion radical in the autoxidation of pyrogallol and a practical assay for superoxide dismutase,” European Journal of Biochemistry, vol.Tetrapropylammonium perruthenate Epigenetic Reader Domain 47, no.PMID:23522542 3, pp. 46974, 1974. [27] J. T. Rotruck, A. L. Pope, H. E. Ganther, A. B. Swanson, D. G. Hafeman, and W. G. Hoekstra, “Selenium: biochemical function as a component of glatathione peroxidase,” Science, vol. 179, no. 4073, pp. 58890, 1973. [28] W. H. Habig and W. B. Jakoby, “[51] Assays for differentiation of glutathione S-Transferases,” Strategies in Enzymology, vol. 77, pp. 39805, 1981. [29] M. S. Moron, J. W. Depierre, and B. Mannervik, “Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver,” Biochimica et Biophysica Acta, vol. 582, no. 1, pp. 678, 1979.
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