• 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.

• ALGAE
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• 제19권4호
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• pp.349-352
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• 2004

We examined MeOH extracts of the marine plants from Korea for their inhibitory activities on rat lens aldose reductase in vitro. Among the MeOH extracts tested, the extracts of Enteromorpha prolifera, Ecklonia cava, Pelvetia siliquosa and Salicornia herbacea exhibited a rat lens aldose reductase inhibition (IC$_{50}$: 3.04, 8.84, 11.42 and 4.99 $\mu$g-ml$^{-1}$, respectively) in vitro.

• 한국식품위생안전성학회:학술대회논문집
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• 한국식품위생안전성학회 2003년도 추계 국제심포지움 및 학술발표회
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• pp.46-46
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• 2003

Hypocholesterolemic peptide isolated from glycimin (11S protein) hydrolyzate by trypsin was purified and identified as LPYP and IAVPGEVA. To investigate the effects of phyiscal properties of side chains of the hypocholesterolemic activity, some of mutant peptides were designed and synthesized chemically. The structure related structures of each peptide were simulated and constructed and their conformations were observed by using spectropolarimeter. The hypocholesterolemic activities were monitored by assaying the inhibition of 3-hydroxy-3-methylglutaryl CoA reductase (HMG-CoA reductase) in vitro and by the determination of cholesterol content in mice serum. For LPYP derivatives, Hypocholesterolemic activity was lost when hydrophobic leucine residue at N-terminus was not so critical for maintaining hypocholesterolemic activity. For idealogical design of hypocholesterolemic peptides, the structure of HMG-CoA reductase are shown and inhibition mechanism of some peptides or inhibitors will be presented. For IAVPGEVA derivative inhibition of HMG-CoA reductase has been studied. For detail study of hypocholesterolemic activity, kinetic study of inhibition of peptides on HMG-CoA reductase and structural view of ligand binding should be investigated.

• 아시안잔디학회지
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• 제1권1호
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• pp.49-55
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• 1987

Zoysia japonica를 부위별로 나누어서 그들간의 amylase와 nitrate reductase의 활성을 조사한 결과는 다음과 같다. 1. Amylase의 활성은 관부에서 8.36~9.46 unit/mg.rotein/hr.로 가장 높았고 이삭에서 2.04 unit/mg.rotein/hr.로 가장 낮았다. 포복경, 뿌리, 잎에서의 amylase의 활성을 각각 5.42~5.82, 3.76, 2.32~3.16 unit/mg.rotein/hr.나타내었다. 2. Nirate reductase의 활성은 빛을 많이 받는 잎에서 0.35~0.66 n mole/mg.rotein/hr.로 가장 높았고 관부에서 0.06~0.10 n mole/mg.rotein/hr.로 가장 낮았다. 이삭과 포복경에서는 각각 0.31,0.27~0.63 n mole/mg.rotein/hr.를 나타내었다. 이러한 결과로부터 저장기관인 관부나 관부 절간에서 높은 amylase의 활성을 이용하여, 양분을 이삭으로 이동시키고 있음을 알 수 있었다. nitrate reductase의 활성은 chloroplast를 갖지 않는 기관보다 광합성기관에서 더 높았다. 잔디밭에서 같이 사는 크로버와 비교해 보면 amylase의 활성이 Zoysia japonica보다 2배가량 더 높았다. 이러한 결과로부터 잔디밭에서 크로버가 더 생장력이 큼을 알 수 있었다.

• 식물조직배양학회지
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• 제28권2호
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• pp.87-90
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• 2001

배추 유래의 cytosolic glutathione reductase 유전자 (BcGR1)의 지속적 발현과 형질전환 식물체의 oxidative stress에 대한 내성과의 관계를 분석하기 위하여, BcGR1 유전자를 CaMV 35S promoter의 하류에 연결한 다음, 담배에 형질전환하였다. PCR 및 Southern blot 분석을 통하여 BcGR1 유전자가 정상적으로 삽입된 32 계통의 T$_{0}$ 식물체를 선발하였다. Northern blot 분석 결과, 도입된 유전자가 형질 전환 식물체 내에서 항상적으로 발현된다는 것을 확인하였으며, 도입 유전자의 copy number와 발현량 사이에는 정의 상관관계를 보이지 않았다.

• Journal of Acupuncture Research
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• 제17권1호
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• pp.129-142
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• 2000

Gamdutang aqua-acupuncture solution(GAS), Gamdutang water-extracted solution(GWS) and Degamdutang aqua-acupuncture solution(DGAS) were prepared and tested for potential antitumor activities. It was used three biomarkers (quinone reductase, omithine decarboxylase, glutathione) to test chemopreventive potentials of GAS, GWS, DGAS. GAS was potent inducer of quinone reductase activity in Hepalclc7 murine hepatoma cells in culture, whereas GWS is less potent. GAS, GWS and DGAS were significantly induced quinone reductase activity in cultured rat normal liver cell, Ac2F. Glutathione levels were increased about 1.8-fold with GAS, 1.0-1.1 fold with GWS, DGAS in cultured murine hepatoma hepaiclc7 cells. In addition glutathione s-transferase levels were increased with GAS, GWS and DGAS. The effects of GAS, GWS and DGAS were tested on the growth of Acanthamoeba castellanii. Proliferation of Acanthamoeba castellanii was inhibited by GAS, GWS and DGAS at concentradons of $1{\times}$ and $5{\times}$. These results suggest that GAS has chemopreventive potential by inducing quinone reductase and quinone reductase activities, inhibition of ornithine decarboxylase activity, and increasing glutathione levels.

• 생약학회지
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• 제32권4호통권127호
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• pp.269-273
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• 2001

Ethanol extracts from Xanthii Fructus (XFE) and Prunellae Spica (PSE) were investigated for the effects on the induction of cancer chemoprevention-associated enzymes. The following effects were measured: (a) induction of quinone reductase (QR) (b) induction of glutathione S-transferase (GST) (c) reduced glutathione (GSH) level. XFE and PSE were potent inducers of quinone reductase activity in Hepa1c1c7 murine hepatoma cells. Glutathione levels were increased with XFE and PSE. In addition, glutathione S-transferase activity was increased with XFE. However, GST activity was not increased with PSE. These results suggest that XFE and PSE have chemopreventive potentials by inducing quinone reductase and increasing GSH levels.

• Journal of Microbiology and Biotechnology
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• 제25권11호
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• pp.1810-1818
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• 2015

For the synthesis of various pharmaceuticals, chiral alcohols are useful intermediates. Among them, (R)-ethyl-4-chloro-3-hydroxybutanoate ((R)-ECHB) is an important building block for the synthesis of L-carnitine. (R)-ECHB is produced from ethyl-4-chloro-3-oxobutanoate (ECOB) by a reductase-mediated, enantioselective reduction reaction. The Saccharomyces cerevisiae YOL151W reductase that is expressed in Escherichia coli cells exhibited an enantioselective reduction reaction toward ECOB. By virtue of the C-terminal His-tag, the YOL151W reductase was purified from the cell-free extract using Ni²⁺-NTA column chromatography and immobilized onto Ni²⁺-magnetic microparticles. The physical properties of the immobilized reductase (Imm-Red) were measured using electron microscopy, a magnetic property measurement system, and a zeta potential system; the average size of the particles was approximately 1 μm and the saturated magnetic value was 31.76 emu/g. A neodymium magnet was used to recover the immobilized enzyme within 2 min. The Imm-Red showed an optimum temperature at 45℃ and an optimum pH at 6.0. In addition, Bacillus megaterium glucose dehydrogenase (GDH) was produced in the E. coli cells and was used in the coupling reaction to regenerate the NADPH cofactor. The reduction/oxidation coupling reaction composed of the Imm-Red and GDH converted 20 mM ECOB exclusively into (R)-ECHB with an e.e._p value of 98%.

• Journal of Microbiology and Biotechnology
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• 제13권5호
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• pp.725-730
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• 2003

Three recombinant Saccharomyces cerevisiae strains showing different levels of xylose reductase activity were constructed to investigate the effects of xylose reductase activity and glucose feed rate on xylitol production. Conversion of xylose to xylitol is catalyzed by xylose reductase of Pichia stipitis with cofactor NAD(P)H. A two-substrate fermentation strategy has been employed where glucose is used as an energy source for NADPH regeneration and xylose as substrate for xylitol production. All recombinant S. cerevisiae strains Yielded similar specific xylitol productivity, indicating that xylitol production in the recombinant S. cerevisiae was more profoundly affected by the glucose supply and concomitant It generation of cofactor than the xylose reductase activity itself. It was confirmed in a continuous culture that the elevation of the glucose feeding level in the xylose-conversion period enhanced the xylitol productivity in the recombinant S. cerevisiae.