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• W2000745821 abstract "Mitochondrial thioredoxin-glutathione reductase was purified from larval Taenia crassiceps (cysticerci). The preparation showed NADPH-dependent reductase activity with either thioredoxin or GSSG, and was able to perform thiol/disulfide exchange reactions. At<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msup><mml:mrow><mml:mn>25</mml:mn></mml:mrow><mml:mrow><mml:mo>∘</mml:mo></mml:mrow></mml:msup><mml:mtext>C</mml:mtext></mml:math>specific activities were<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mn>437</mml:mn><mml:mi> </mml:mi><mml:mo>±</mml:mo><mml:mi> </mml:mi><mml:mn>27</mml:mn></mml:math>mU mg -1 and<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mn>840</mml:mn><mml:mi> </mml:mi><mml:mo>±</mml:mo><mml:mi> </mml:mi><mml:mn>49</mml:mn></mml:math>mU mg -1 with thioredoxin and GSSG, respectively. Apparent<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msub><mml:mrow><mml:mtext>K</mml:mtext></mml:mrow><mml:mrow><mml:mtext>m</mml:mtext></mml:mrow></mml:msub></mml:math>values were<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mn>0.87</mml:mn><mml:mi> </mml:mi><mml:mo>±</mml:mo><mml:mi> </mml:mi><mml:mn>0.04</mml:mn><mml:mi> </mml:mi></mml:math>μM,<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mn>41</mml:mn><mml:mi> </mml:mi><mml:mo>±</mml:mo><mml:mi> </mml:mi><mml:mn>6</mml:mn><mml:mi> </mml:mi></mml:math>μM and<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mn>19</mml:mn><mml:mi> </mml:mi><mml:mo>±</mml:mo><mml:mi> </mml:mi><mml:mn>10</mml:mn><mml:mi> </mml:mi></mml:math>μM for thioredoxin, GSSG and NADPH, respectively. Thioredoxin from eukaryotic sources was accepted as substrate. The enzyme reduced H 2 O 2 in a NADPH-dependent manner, although with low catalytic efficiency. In the presence of thioredoxin, mitochondrial TGR showed a thioredoxin peroxidase-like activity. All disulfide reductase activities were inhibited by auranofin, suggesting mTGR is dependent on selenocysteine. The reductase activity with GSSG showed a higher dependence on temperature as compared with the DTNB reductase activity. The variation of the GSSG- and DTNB reductase activities on pH was dependent on the disulfide substrate. Like the cytosolic isoform, mTGR showed a hysteretic kinetic behavior at moderate or high GSSG concentrations, but it was less sensitive to calcium. The enzyme was able to protect glutamine synthetase from oxidative inactivation, suggesting that mTGR is competent to contend with oxidative stress." @default.
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• W2000745821 date "2010-01-01" @default.
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• W2000745821 title "Mitochondrial Thioredoxin-Glutathione Reductase from LarvalTaenia crassiceps(Cysticerci)" @default.
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• W2000745821 doi "https://doi.org/10.1155/2010/719856" @default.
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