• Preventive Nutrition and Food Science
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• 제14권4호
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• pp.358-361
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• 2009

Aldose reductase was purified to electrophoretic homogeneity from porcine liver. The purified enzyme was a monomer of 36 kDa. The enzyme was strongly inhibited by $Cu^{2+}\;and\;Mg^{2+}$ ions. Incubation of the enzyme with pyridoxal 5'-phosphate led to complete inhibition of enzymatic activity, suggesting that lysine residue is involved at or near the active site of the enzyme. The enzyme exhibited a broad substrate specificity. Furthermore, the enzyme was capable of decolorizing Alizarin, an anthraquinone dye.

• 생약학회지
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• 제32권3호통권126호
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• pp.248-252
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• 2001

The present study was undertaken to elucidate the hypoglycemic effect and inhibitory effect of Cudrania tricuspidata root bark on aldose reductase activity. C. tricuspidata MeOH ext. 1,000 mg/kg showed a significant blood glucose lowering effect on alloxan-induced hyperglycemic rats and increasing body weight. C. tricuspidata MeOH ext. showed a potent inhibitory effect on bovine lens aldose reductase.

• 한국식품과학회지
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• 제38권5호
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• pp.691-698
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• 2006

본 연구는 혈액순환 개선 효능을 알아보기 위해 민간에서 빈번하게 사용하는 허브류인 마조람, 라벤더, 딜, 로즈마리, 히솝, 장미, 레몬밤, 파인애플 세이지 및 에키네시아 등 총 9종 을 실험 시료로 선정하였다. 이들을 부위별 및 용매별로 추출하여 angiotensin I converting enzyme(ACE) 저해 활성, hydroxy-methylglutalyl coenzyme A reductase 저해활성 및 혈전용해활성을 측정하였다. 추출 수율은 장미꽃이 가장 높았으며 열수 추출의 경우 43.3%였고 70% 에탄올 추출의 경우 45%였다. ACE 저해활성은 열수 추출의 경우 장미꽃이 133.8% 로 가장 높았고 70% 에탄올 추출의 경우에는 파인애플 세이지 잎이 91.2%로 가장 높았다. HMG-CoA reductase 저해활성의 경우에는 장미꽃이 열수 추출물 48.9%, 70% 에탄올 추출물 80.5%로 모두 높았다. 혈전용해활성도 장미꽃에서 열수 추출이나 에탄올 추출물 모두 가장 높은 활성을 보였다. 이상의 결과로 볼 때 장미꽃 추출물의 혈액순환 개선 효과가 뛰어난 것으로 나타나 기능성 식품으로의 개발 가능성이 기대된다.

• Journal of Plant Biotechnology
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• 제3권1호
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• pp.13-17
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• 2001

A Chromium (VI)[Cr(VI)] reductase gene from heavy metal reducing bacteria Pseudomonas aeruginosa HP014 was used to transform tobacco plant cells. A chimeric construct containing the Cr(VI) reductase gene was transfered to tobacco leaf disks using an Agrobacteriun tumefaciens binary vector system. From the leaf disks, transformed plantlets were regenerated. Hybridization experiments demonstrated that the Cr(VI) reductase gene was inserted into and expressed in the regenerated plants. The Cr(VI) reduction activity showed that the transgenic plants may be a another possible tool to reduce the pollution of the toxic Cr(VI) in soil.

• BMB Reports
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• 제33권4호
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• pp.321-325
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• 2000

Quinone reductase was purified to homogeneity from bovine liver by using ammonium sulfate fractionation, ionexchange chromatography, and gel filtration chromatography. The enzyme utilized either NADH or NADPH as the electron donor. The enzyme catalyzed the reduction of several quinones and other artificial electron acceptors. Furthermore, the enzyme catalyzed NAD(P)H-dependent reduction of azobenzene. The apparent Km for 1,4-benzoquinone and azobenzene was 1.64 mM and 0.524 mM, respectively. The reduction of azobenzene by quinone reductase was almost entirely inhibited by dicumarol or Cibacron blue 3GA, potent inhibitors of the mammalian quinone reductase. In the presence of 1.0${\mu}M$ Cibacron blue 3GA, azoreductase activity was lowered by 45%, and almost complete inhibition was seen above 2.0 ${\mu}M$ Cibacron blue 3GA.

• BMB Reports
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• 제32권3호
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• pp.254-258
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• 1999

The NADPH-dependent succinic semialdehyde reductase is one of the key enzymes in the brain GABA shunt, and it catalyzes the formation of the neuromodulator $\gamma$-hydroxybutyrate from succinic semi aldehyde. This enzyme was inactivated by diethylpyrocarbonate (DEP) with the second-order rate constant of $1.1{\times}10^3\;M^{-1}min^{-1}$ at pH 7.0, $25^{\circ}C$, showing a concomitant increase in absorbance at 242 nm due to the formation of N-carbethoxyhistidyl derivatives. Complete inactivation of succinic semialdehyde reductase required the modification of five histidyl residues per molecule of enzyme. However, only one residue was calculated to be essential for enzyme activity by a statistical analysis of the residual enzyme activity. The inactivation of the enzyme by DEP was prevented by preincubation of the enzyme with the coenzyme NADPH but not with the substrate succinic semialdehyde. These results suggest that an essential histidyl residue involved in the catalytic activity is located at or near the coenzyme binding site of the brain succinic semialdehyde reductase.

• Journal of Microbiology
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• 제45권4호
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• pp.333-338
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• 2007

Intracellular NADH:quinone reductase involved in degradation of aromatic compounds including lignin was purified and characterized from white rot fungus Trametes versicolor. The activity of quinone reductase was maximal after 3 days of incubation in fungal culture, and the enzyme was purified to homogeneity using ion-exchange, hydrophobic interaction, and gel filtration chromatographies. The purified enzyme has a molecular mass of 41kDa as determined by SDS-PAGE, and exhibits a broad temperature optimum between $20-40^{\circ}C$, with a pH optimum of 6.0. The enzyme preferred FAD as a cofactor and NADH rather than NADPH as an electron donor. Among quinone compounds tested as substrate, menadione showed the highest enzyme activity followed by 1,4-benzoquinone. The enzyme activity was inhibited by $CuSO_4,\;HgCl_2,\;MgSO_4,\;MnSO_4,\;AgNO_3$, dicumarol, KCN, $NaN_3$, and EDTA. Its $K_m\;and\;V_{max}$ with NADH as an electron donor were $23{\mu}M\;and\;101mM/mg$ per min, respectively, and showed a high substrate affinity. Purified quinone reductase could reduce 1,4-benzoquinone to hydroquinone, and induction of this enzyme was higher by 1,4-benzoquinone than those of other quinone compounds.

• 한국작물학회지
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• 제33권3호
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• pp.209-214
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• 1988

질소비료의 증비와 숙도의 차이가 버어리종 잎담배의 수량과 품질 및 내용성분에 미치는 영향을 시험한 결과는 다음과 같다. 1. 질소비료가 증가될수록 건조엽의 적색도가 증가되었고, 2. 엽분별 수확시기를 보면 하위엽은 미숙엽에서, 상위엽은 과숙엽에서 수확할 때 kg당 가격이 가장 낮았다. 3. 미숙엽과 과숙엽은 수량이 대등하였으나 과숙엽은 수량이 떨어졌다. 4. 질소비료의 증비와 숙도에 따른 단백질 pattern의 차이는 나타나지 않았다. 5. 생육후기에는 비료수분 및 숙도에 따른 Nitrate reductase 활성도에는 차이가 나타나지 않았다.

• BMB Reports
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• 제42권9호
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• pp.580-585
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• 2009

Dimethyl sulfoxide (DMSO) is widely used in chemistry and biology as a solvent and as a cryoprotectant. It is also used as a pharmaceutical agent for the treatment of interstitial cystitis and rheumatoid arthritis. Previous reports described DMSO as being reduced by methionine-S-sulfoxide reductase (MsrA). However, little is known about the DMSO reduction capability of methionine-R-sulfoxide reductase (MsrB) or its effect on the catalysis of methionine sulfoxide reduction. We show that mammalian MsrB2 and MsrB3 were unable to reduce DMSO. This compound inhibited MsrB2 activity but did not inhibit MsrB3 activity. We further determined that DMSO functions as an inhibitor of MsrA and MsrB2 in the reduction of methionine sulfoxides via different inhibition mechanisms. DMSO competitively inhibited MsrA activity but acted as a non-competitive inhibitor of MsrB2 activity. Our study also demonstrated that DMSO inhibits in vivo methionine sulfoxide reduction in yeast and mammalian cells.

• Archives of Pharmacal Research
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• 제26권11호
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• pp.951-959
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• 2003

A series of typical (chlorpromazine, haloperidol and thioridazine) and atypical (risperidone, quetiapine, clozapine and olanzapine) antipsychotics were tested for effects on integrated bioenergetic functions of isolated rat liver mitochondria. Polarographic measurement of oxygen consumption in freshly isolated mitochondria showed that electron transfer activity at respiratory complex I is inhibited by chlorpromazine, haloperidol, risperidone, and quetiapine, but not by clozapine, olanzapine, or thioridazine. Chlorpromazine and thioridazine act as modest uncouplers of oxidative phosphorylation. The typical neuroleptics inhibited NADH-coenzyme Q reductase in freeze-thawed mitochondria, which is a direct measure of complex I enzyme activity. The inhibition of NADH-coenzyme Q reductase activity by the atypicals risperidone and quetiapine was 2-4 fold less than that for the typical neuroleptics. Clozapine and olanzapine had only slight effects on NADH-coenzyme Q reductase activity, even at 200 $\mu$ M. The relative potencies of these neuroleptic drugs as inhibitors of mitochondrial bioenergetic function is similar to their relative potencies as risk factors in the reported incidence of extrapyramidal symptoms, including tardive dyskinesia (TD). This suggests that compromised bioenergetic function may be involved in the cellular pathology underlying TD.