GSSG reductase recycling cid. The proteasome inhibitors concentration of the reduced GSH in the sample was obtained by subtracting GSSG GSH were obtained T. Both concentrations of reduced GSH and GSSG calculated from the formula and expressed as nmol / mg protein. The activity Th of GPx, GR was SOD, CAT and measured in the cell lysate by standard chemical methods colorimetric tests using commercial kits. GPx activity t was determined by quantifying the rate of oxidation of reduced glutathione to oxidized glutathione on the catalysis. GSH reacts with 5, 5 dithiobis pnitrobenzoic Acid Yellow and produces compounds which can be detected at 412 nm using a spectrophotometer. This was done to sentieren the reduction of GSH to repr. One unit of enzyme activity t was in this case the reduction of 1 mole per minute per 1 mg protein defined GSH, GSH was removed after the reduction of non-enzymatic reaction. The enzyme activity t was expressed as U / mg protein. GR activity t was described using the method of Carlberg and Mannervik. Glutathione reductase for NADPH-dependent Ngigen conversion of oxidized glutathione into high throughput screening reduced glutathione is required. The exponential decay of NADPH was detected by spectrophotometry at 340 nm. One unit of enzyme activity t was here as the oxidation of 1 mol / L NADPH per minute per 1 mg protein. The enzyme activity, t is expressed in U / mg protein. SOD activity was t ability by its R, Measured generates the reduction of nitro blue tetrazolium by superoxide ions by the xanthine / xanthine oxidase system inhibit. The size E of the reduction of NBT was followed spectrophotometrically by measuring absorbance at 560 nm. One unit of the SOD activity was t as the amount of enzyme capable of causing 50% inhibition in L Solution at 1 ml reaction per milligram protein. The enzyme activity t was expressed as U / mg protein. CAT activity t was determined by measuring the intensity t of a complex with the yellow and molybdate H2O2 is formed at 405 nm after the ammonium was added to terminate the reaction catalyzed decomposition of H2O2 detected CAT.
One unit of enzyme activity t was here as the reduction of 1 mol H2O2 per second per mg protein. The enzyme activity t was CCR5 expressed as U / mg protein. The protein content of the cell lysate was prepared by Herk Mmliche method determined. NF NF activity t activity t was determined using a transcription factor NF TransAMTM p65 assay kit according to the manufacturer S instructions. The kit contains Lt 96 well plates to which oligonucleotides containing a consensus NF binding site. The activated NF contained in nuclear extracts was being capable of specifically binding to these oligonucleotides. It was rpern using specific antibody. Five micromoles Bay 117 082 was used as controlled Positive for the inhibition of NF . Statistical analysis The results were recorded as mean ± SD. Physiological and biochemical parameters were analyzed statistically using analysis of variance with Dunnet ttesting on Ver changes Followed to evaluate between the groups. P 0.05 was considered significant, P 0.01 was considered very important. Results BP5 has an inhibitory effect on NO production to determine whether the protective effect of BP5 were exercised by a mediation NO, the amount of NO produced by macrophages is measured. LPS significantly induced the production of NO.