Uchirappalli, Tamilnadu, India, for providing the Piper betle wide variety.Evidence-Based Complementary and Option Medicine[15] Globe Health Organization, “FAO/WHO specialist committee on food additives evaluation of certain food additives and contaminants,” Tech. Rep. 683, WHO, Geneva, Switzerland, 1982. [16] A. M. Rimando, B. H. Han, J. H. Park, and M. C. Casein Kinase Purity & Documentation 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. 2, 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 fast and sensitive process for the quantitation of microgram quantities of protein using the principle of protein dye binding,” Analytical Biochemistry, vol. 72, no. 1-2, pp. 24854, 1976. [20] T. Sasaki, S. Matzy, along with a. Sonal, “Effect of acetic acid concentration on the colour reaction in the O-toluidine boric acid technique 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 {ERRβ supplier plasma, devoid of use on the preparative ultracentrifuge,” Clinical Chemistry, vol. 18, no. 6, pp. 49902, 1972. [22] J. 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 Practical 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. 2, pp. 38994, 1972. [26] S. Marklund and G. Marklund, “Involvement of your superoxide anion radical inside the autoxidation of pyrogallol in addition to a hassle-free assay for superoxide dismutase,” European Journal of Biochemistry, vol. 47, no. three, 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 part as a element 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,” Methods 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. [30] S. T. Omaye, J. David Turnbull, and H. E. Sauberlich, “[1] Selected solutions for the determination of ascorbic acid in animal cells, tissues, and fluids,” Strategies in Enzymology, vol. 62, pp. 31, 1979. [31] I. D. Desai, “Vitamin E evaluation approaches for animal tissues,” Techniques in Enzymology, vol. 105, pp. 13847, 1984. [32] H. Ohkawa, N. Ohishi, and K. Yagi, “Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction,” Analytical Biochemistry, vol. 95, no. 2, pp. 35158, 1979.
Anatom.