Ressed in SOD units/mg of total protein.Determination of catalase activity (CAT)This technique is based in the interaction between the coomassie brilliant blue pigment BG 250 (Sigma-Aldrich? SP, Brazil) and the protein macromolecules that contain aromatic or basic lateral amino acids. The interaction PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/26866270 between the high molecular weight protein and the pigment provokes a shift of this in the equilibrium to the anionic form, which absorbs strongly at 595 nm [22]. To assess the dosage of protein in the tissue, 10 l of homogenized sample was diluted in 190 l of distilled water. Twenty microliters of this solution was placed in plastic cuvettes (order Lixisenatide optical path: 10 mm), containing 1 ml of Bradford reagent. The sample absorbances were determined at 595 nm, in a Lambda 35 spectrophotometer (Perkin-Elmer of Brazil, SP, Brazil). The protein standard curve was obtained from known concentrations of standard solutions of bovine albumin (1 mg/ml).Determination of malondialdehyde (MDA) through the thiobarbituric acid reactive substances testThe CAT activity was determined through the decomposition of hydrogen peroxide at 25 . In a quartz cuvette, 2865 l of phosphate buffer 50 mM (pH 7.0) and 30 l of homogenized tissue or plasmatic supernatant were added. Then, 35 l of 0.02 M hydrogen peroxide was added to the solution. The sample absorbances were determined in a Lambda 35 spectrophotometer (PerkinElmer of Brazil, SP, Brazil), at 240 nm, and the results are expressed in pmol/mg of total protein [25].Statistical analysisTo determine the MDA concentration, the technique according to JA Buege and SD Aust [23]. To promote the precipitation of proteins, 125 l of tissue homogenate or plasmatic supernatant was added to 375 l of 10 trichloroacetic acid solution. Next, the samples were centrifuged (3,000 rpm for 10 minutes at 6 ) and 250 l of 0.670 thiobarbituric acid was added to 250 l of supernatant. The solution was agitated and heated at 100 in a water-bath for 15 minutes. After cooling, 750 l of n-butanol was added. Then, following the second agitation, the samples were centrifuged (3,000 rpm for 5 minutes at 6 ). The stained supernatant was placed in glass microcuvettes to determine the absorbance at 535 nm in a Lambda 35 spectrophotometer (Perkin-Elmer of Brazil, SP,The data were evaluated using the software SigmaPlot version 12.0 for Windows. To detect a minimal difference of 18.91 , with an alpha error of 5 and a power of 80 , the minimal number of animals calculated to be required for each group was ten. This difference was based on a previous study in our laboratory, which utilized an outcome of maximum strength gain (Alves JP, personal communication, 2011). The results were expressed as the mean ?SD. Here, the two-way ANOVA test followed by the StudentNewman-Keuls’ Post Hoc test was used to make comparisons among groups. For associations among variables, the Pearson Correlation Test was performed. The accepted significance level was 5 (P < 0.05). For sample size calculations, the software SigmaPlot version 12.0 for Windows was utilized. To perform correlations and graphics, the software GraphPad 5.0 for Windows was used.Results The body weight of the animals at the beginning of the study was similar (P > 0.05), but was different by the end. The trained groups demonstrated lower body weight gainStefani et al. Journal of the International Society of Sports Nutrition 2014, 11:11 http://www.jissn.com/content/11/1/Page 4 ofwhen compared to the SED-Cr gr.