• The Journal of Natural Sciences
• /
• v.14 no.2
• /
• pp.55-65
• /
• 2004

A thiol-specific antioxidant(TSA) protein was purified from Earthworm, Lumbricus terrestris by DEAE-Cellulose, Phenl sepharose, Sephacryl S-200 gel filtration and HPLC S-300 Column Chromatography. This protein showed a thiol-specific antioxidant activity against inactivation of glutamine synthetase by a metal-catalysed oxidation system capable of generation reaction oxygen species. The molecular mass of the protein was determinated to be 51-kDa by SDS-polyacrylamide gel electrophores. Taken together, the purified TSA protein could be a new member of TSA family.

• Korean Chemical Engineering Research
• /
• v.46 no.6
• /
• pp.1148-1152
• /
• 2008

Molten carbonate oxidation (MCO) is one of the promising alternative technologies for the treatment of the chlorinated organic compounds because it is capable of trapping chlorine during a destruction of them. In this study, destructions of chlorinated organic compounds ($C_6H_5Cl$, $C_2HCl_3$ and $CCl_4$) and an insulated oil containing PCBs were performed by using the two stage molten carbonate oxidation system. MCO reactor temperature largely affected the destruction of the chlorinated organic compounds. Destruction of the chlorinated organics very efficient in the primary MCO reactor however a significant amount of CO was emitted from the MCO system. This CO emission was gradually decreased by an increase in the primary reactor temperature and oxidizing air feed rate. The HCl emission from the MCO system was below 7 ppm regardless of tested conditions. The chlorine collection efficiencies were in the range of 99.95-99.99%. The destruction of PCBs in the insulated oil was efficient at a temperature above $900^{\circ}C$ and overall destruction efficiency of them was determined as over 99.9999%.

• Journal of Sensor Science and Technology
• /
• v.7 no.5
• /
• pp.319-326
• /
• 1998

Anodic half-reaction in the $Na^+$ ionic sensors using $Na_2CO_3$ and $MCO_3$ ($M=Cs_2,K_2,Li_2,Ca$) as a sensitive membrane is derived in continuous flow system to explain $CO_2$ sensing characteristics. For various gas-sensitive membranes, a well known overall reaction, $MCO_3\;=\;MO\;+\;CO_2$, cannot be applied for the EMF behaviors of these kinds of sensors. So, the anodic reaction is found to involve $Na_2CO_3$ and $M^{++}$-containing oxide phases by employing the ion exchange reaction at the interface of solid electrolyte and the sensitive membrane to maintain ionic balance in the whole cell. Based on the electrode reaction derived in flow system, differences of cell potentials between continuous and discontinuous flow systems were also discussed. These EMF differences were considerably caused by the partial pressures of oxygen and $CO_2$ as well as irreversible chemical reactions between electrode materials and $CO_2$ atmosphere.

• Biomedical Science Letters
• /
• v.4 no.1
• /
• pp.1-9
• /
• 1998

A Corynebacterium diphtheriae iron-repressible gene dirA, that was homologous to TSA of Saccharomyces cerevisiae and AhpC subunit of Salmonella typhimurium alkyl hydroperoxide reductase, was amplified with PCR and expressed in E. coli. The DirA purified from the transformed E. coli crude extracts prevented the inactivation of enzyme caused by metal-catalyzed oxidation (MCO) system containing thiols but not by ascorbate/Fe$^{3+}$/$O_2$ MCO system. The DirA concentration, which inhibited the inactivation of glutamine synthetase by 50% (IC$_{50}$) against MCO system, was 0.12 mg/ml. The multimeric forms of DirA were converted to the monomeric form in SDS-PAGE under the thioredoxin system comprised of NADPH, Saccharomyces cerevisiae thioredoxin reductase, and thioredoxin. Also, DirA showed thioredoxin dependent peroxidase activity. All of these results were consistent with the characteristics of a thiol specific antioxidant (TSA) protein having two conserved cysteine residues.

• BMB Reports
• /
• v.28 no.3
• /
• pp.249-253
• /
• 1995

The nonenzymatic glycation of copper, zinc-superoxide dismutase (Cu,Zn-SOD) led to inactivation and fragmentation of the enzyme. The glycated Cu,zn-SOD was isolated by boronate affinity chromatography. The formation of 8-hydroxy-2'-deoxyguanosine (8-OH-dG) in calf thymus DNA and the generation of strand breaks in pBhiescript plasmid DNA by a metal-catalyzed oxidation (MCO) system composed of $Fe^{3+}$, $O_2$, and glutathione (GSH) as an electron donor was enhanced more effectively by the glycated CU,Zn-SOD than by the nonglycated enzyme. The capacity of glycated Cu,Zn-SOD to enhance damage to DNA was inhibited by diethylenetriaminepentaacetic acid (DETAPAC), azide, mannitol, and catalase. These results indicated that incubation of glycated CU,Zn-SOD with GSH-MCO may result in a release of $Cu^{2+}$ from the enzyme. The released $Cu^{2+}$ then likely participated in a Fenton-type reaction to produce hydroxyl radicals, which may cause the enhancement of DNA damage.

• The Journal of Natural Sciences
• /
• v.14 no.1
• /
• pp.7-24
• /
• 2004

We found new type of thiol peroxidase, fused with GRX.(TPx-GRX) The TPx-GRX exists in pathogenic bacteria including -. This protein was homogeneously purified from the E.coli recombinant overexpressing TPx-GRX. In the presence of a thiol-containing electron donor such as DTT, the purified TPx-GRX has potent the antioxidant to prevent the inactivation of GS by the MCO system, which is comprised of DTT, $Fe^{3+}$, and $O^2$. The antioxidant activity is much higher that other thiol peroxidase. The investigate the peroxidase activity of TPx-GRX, we directly measured the peroxidase activity of TPx-GRX toward peroxides in terms of the removal of peroxides in the presence of GSH. This result demonstrates that the peroxidase activity of TPx-GRX. These taken together results suggest that TPx-GRX is a new member of thiol peroxidase. These observations also suggest that in the pathogenic bacteria, TPx-GRX plays an important antioxidative role as a multiple array defence mechanism against oxidative stress.

• The Journal of Natural Sciences
• /
• v.14 no.2
• /
• pp.67-82
• /
• 2004

A thiol-specific antioxidant protein (TSA or TPx) was purified from Halophilic archeabacteria Halococcus agglomeratus, by DEAE-Cellulose, Phnyl, sepharose, Sephadex G-75, Sephacryl S-100, Sephacryl S-200, and Q-Wepharose FF. This protein exhibited the preventeive effect against the inactivation of glutamine synthehase (GS) activity was support by a thiol-reducing equicalent such as dithiothreitol. TPx activity was maximal at NaCl concentration above 500mM. The molecular mass of the protein was determinated to be 22-kDa by SDS-PAGE. The TPx purified from Halococcus agglomeratus seems to be similar to other TPx family, except for the salt requirement for the maximal antioxidant activity.

• BMB Reports
• /
• v.33 no.6
• /
• pp.514-518
• /
• 2000

Two open reading frames of Haemophilus influenzae, HI0572 and HI0751, showing homology to a yeast thioredoxin peroxidase II (TPx II) and an E. coli thiol peroxidase $P_{20}$, respectively, were cloned and expressed in E. coli, and then the proteins were subsequently purified and characterized. HI0751 protein showed the thioredoxin (Trx)-dependent peroxidase activity, whereas HI0572 protein showed glutathione-dependent peroxidase. The HI0572 is the first peroxiredoxin with glutathione peroxidase activity rather than thioredoxin peroxidase. Purified HI0572 and HI0751 proteins protected specifically the inactivation of glutamine synthetase by metal catalyzed oxidation (MCO) systems composed of $Fe^{3+}$, $O_2$ and mercaptans such as dithiothreitol, ${\beta}-mercaptoethanol$ and glutathione (GSH). Unlike the HI0751 protein, the HI0572 protein was more effective in protecting glutamine synthetase from inactivation by the $GSH/Fe^{3+}/O_2$ system. It seems that these unique properties of the HI0572 protein are due to the structure containing a glutaredoxin domain at it's C-terminal in addition to a peroxiredoxin domain.