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Biochemical Estimation Techniques

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Abstract

Tissues were minced with sharp scissors and then thawed and homogenized with the aid of York’s homogenizer fitted with Teflon plunger in a proportion of 1:10(w/v) ice-cold phosphate buffer (50 mM; PH 7.4). Aliquots of homogenates were used for the determination of malondialdehyde (MDA), hydroperoxides, reduced glutathione (GSH), and total sulfhydryl (TSH) levels. The homogenates were centrifuged for 60 min at 10,000× g at 4 °C, and determination of superoxide dismutase (SOD) and catalase (CAT) activities were carried out with the resultant supernatant. Protein concentration was determined according to the method of Lowry et al. (1951) using purified bovine serum albumin as standard.

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References

  • Aebi H (1984) Catalase in vitro. Methods Enzymol 105:121–126

    Article  CAS  PubMed  Google Scholar 

  • Benzie IFF, Strain JJ (1996) The ferric reducing ability of plasma (FRAP) as a measure of “antioxidant power”: the FRAP assay. Anal Biochem 239:70–76

    Article  CAS  PubMed  Google Scholar 

  • Ellman GL (1959) Tissue sulfhydryl groups. Arch Biochem Biophys 82:70

    Article  CAS  PubMed  Google Scholar 

  • Haldebrandt AG, Roots I (1975) Reduced nicotinamide adenine dinucleotide phosphate (NADPH) dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reaction in liver microsome. Arch Biochem Biophys 171:385–397

    Article  Google Scholar 

  • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with folin phenol reagent. J Biol Chem 193:265–275

    CAS  PubMed  Google Scholar 

  • Marklund S, Marklund G (1974) Involvement of superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem 47:469–474

    Article  CAS  PubMed  Google Scholar 

  • Noro T, Oda Y, Miyase T, Ueno A, Fukushima S (1983) Inhibitors of xanthine oxidase from the flowers and buds of Daphne genkwa. Chem Pharm Bull 31:3984–3987

    Article  CAS  PubMed  Google Scholar 

  • Ohkawa H, Ohishi N, Yagi K (1979) Assay for lipid peroxides in animal tissue by thiobarbituric reaction. Anal Biochem 95:351–358

    Article  CAS  PubMed  Google Scholar 

  • Paglia DE, Valentine WN (1967) Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med 70:158–169

    CAS  PubMed  Google Scholar 

  • Sedlak J, Lindsay RH (1968) Estimation of total, protein-bound and nonprotein sulfhydryl groups in tissue with Ellman’s reagent. Anal Biochem 25:192–205

    Article  CAS  PubMed  Google Scholar 

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Nabi, S. (2014). Biochemical Estimation Techniques. In: Toxic Effects of Mercury. Springer, New Delhi. https://doi.org/10.1007/978-81-322-1922-4_10

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