Stimulatory effect of components of rose flowers on catalytic activity and mRNA expression of superoxide dismutase and catalase in erythrocytes
ABSTRACT In the present study, two antioxidant components (polysaccharopeptide complex P(1-a) and condensed tannin P(1-b)) from rose (Rosa rugosa) flowers were each incubated with mouse erythrocytes to investigate their effect on erythrocyte superoxide dismutase (SOD), and catalase (CAT) activities. It was found that the activities of Cu, Zn-SOD and CAT were markedly increased after incubation for 3h with rose flower fractions at the concentration of 500μg/ml. Similar changes were also observed in the erythrocyte gene expression of SOD and CAT. These results show that P(1-a) and P(1-b) are effective antioxidants that increase the activity and the gene expression of SOD and CAT in mouse erythrocytes.
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ABSTRACT: 4-Aminoantipyrine (AAP) is scarcely administered as an analgesic drug because of side effects. The residue of AAP in the environment is potentially harmful. To evaluate the toxicity of AAP from molecular level, the effects of AAP on the important antioxidant enzyme copper-zinc superoxide dismutase (Cu/ZnSOD) were explored using spectroscopic and molecular modeling methods. AAP can spontaneously bind with Cu/ZnSOD with one binding site to form AAP-Cu/ZnSOD complex through hydrogen bond and van der Waals forces. The molecular docking simulation revealed that AAP bound into the Cu/ZnSOD interface of two subdomains, which induced some conformational and microenvironmental changes of Cu/ZnSOD and further caused the inhibition of Cu/ZnSOD activity. The present study provides important insights into toxic mechanism of AAP with Cu/ZnSOD. The estimated research route can be applied to characterize interactions of enzyme systems and other pollutants and drugs.Journal of hazardous materials 08/2013; 262C:318-324. DOI:10.1016/j.jhazmat.2013.08.047 · 4.33 Impact Factor
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ABSTRACT: The interactions between well-dispersed multiwalled carbon nanotubes (MWCNTs) and catalase (CAT) were investigated. The activity of CAT was inhibited with the addition of MWCNTs. After deducting the inner filter effect, the fluorescence spectra revealed that the tryptophan (Trp) residues were exposed and the fluorescence intensities of CAT increased with the increase in the MWCNTs concentration. At the same time, the environment of the Trp residues became more hydrophobic. The results of UV–vis absorption spectroscopy and CD spectra indicated that the secondary structure of CAT had been changed, and the amino acid residues were located in a more hydrophobic environment. Meanwhile, the UV–vis spectra indicated that the conformation of the heme porphyrin rings was changed. The microenvironment of CAT activity sites may be interfered by MWCNTs. This research showed that MWCNTs could not only contribute to the conformational changes of protein but also change the enzyme function.Journal of Biochemical and Molecular Toxicology 05/2014; 28(5). DOI:10.1002/jbt.21555 · 1.32 Impact Factor
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ABSTRACT: The full-length cDNA of Pleurotus ostreatus superoxide dismutase (PoMn-SOD) was cloned and successfully expressed by using the pPIC9K vector under the control of alcohol oxidase 1 promoter with a secretion signal peptide (α-factor) in Pichia pastoris. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting demonstrated that recombinant PoMn-SOD, a 21.8 kDa protein, was secreted into the culture medium. Nondenaturing PAGE experiments confirmed that recombinant PoMn-SOD was secreted in a functionally active form and the expression system did not require any acid activation process. The factors affecting the expression level were optimized in shaking flask cultures. The maximum enzyme activity (156.9 U/mg) was observed under the following conditions: Initial medium pH was 6.0, induction time point was at the 6th day, and methanol concentration was 0.7 % (v/v). This was the first report on secretory expression of recombinant PoMn-SOD in P. pastoris, which might provide a reference for further practical applications.Applied Biochemistry and Biotechnology 07/2014; 174(1). DOI:10.1007/s12010-014-1057-1 · 1.69 Impact Factor