• Advances in Traditional Medicine
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• 제9권1호
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• pp.49-57
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• 2009

The antifertility activity of methanol extract of Cuscuta reflexa Roxb. stem (MECR) and Corchorus olitorius Linn. seed (MECO) were studied on male Swiss albino mice. The extracts were found to decrease sperm count, percentage of motile sperm and testosterone level in treated mice when compared with vehicle control after 17 days of treatment. The weight of gonads, epididymis were decreased whereas no significant changes of the body weight of mice were observed after methanol extract treatments. The fertility test showed 100% negative result in MECR and MECO treated mice at medium and high dose level of treatment. MECR and MECO in low (25 mg/kg and 15 mg/kg, respectively), medium (50 mg/kg and 20 mg/kg, respectively) and high (75 mg/kg and 25 mg/kg, respectively) dose level caused a simultaneous fall in testicular ${\Delta}5$-$3{\beta}$-hydroxy steroid dehydrogenase and glucose-6-phosphate dehydrogenase activities which are involved in testicular steroidogenesis. Total cholesterol and ascorbic acid content in testis were increased significantly in gonads. The activities of lactate dehydrogenase, malic dehydrogenase and ascorbic acid oxidase were reduced whereas that of carbonic anhydrase was increased significantly in the testis of MECR and MECO treated mice. All these observations indicate that the methanol extract of C. reflexa stem and C. olitorius seed produced antifertility activity in sexually matured male mice, which may be due to inhibition of gonadal steroidogenesis. This activity may be attributed due to the presence of flavonoids and steroids, respectively.

• Journal of Microbiology and Biotechnology
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• 제31권5호
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• pp.756-763
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• 2021

Agarose is a linear polysaccharide composed of ᴅ-galactose and 3,6-anhydro-ʟ-galactose (AHG). It is a major component of the red algal cell wall and is gaining attention as an abundant marine biomass. However, the inability to ferment AHG is considered an obstacle in the large-scale use of agarose and could be addressed by understanding AHG catabolism in agarolytic microorganisms. Since AHG catabolism was uniquely confirmed in Vibrio sp. EJY3, a gram-negative marine bacterial species, we investigated AHG metabolism in Streptomyces coelicolor A3(2), an agarolytic gram-positive soil bacterium. Based on genomic data, the SCO3486 protein (492 amino acids) and the SCO3480 protein (361 amino acids) of S. coelicolor A3(2) showed identity with H2IFE7.1 (40% identity) encoding AHG dehydrogenase and H2IFX0.1 (42% identity) encoding 3,6-anhydro-ʟ-galactonate cycloisomerase, respectively, which are involved in the initial catabolism of AHG in Vibrio sp. EJY3. Thin layer chromatography and mass spectrometry of the bioconversion products catalyzed by recombinant SCO3486 and SCO3480 proteins, revealed that SCO3486 is an AHG dehydrogenase that oxidizes AHG to 3,6-anhydro-ʟ-galactonate, and SCO3480 is a 3,6-anhydro-ʟ-galactonate cycloisomerase that converts 3,6-anhydro-ʟ-galactonate to 2-keto-3-deoxygalactonate. SCO3486 showed maximum activity at pH 6.0 at 50℃, increased activity in the presence of iron ions, and activity against various aldehyde substrates, which is quite distinct from AHG-specific H2IFE7.1 in Vibrio sp. EJY3. Therefore, the catabolic pathway of AHG seems to be similar in most agar-degrading microorganisms, but the enzymes involved appear to be very diverse.

• 미생물학회지
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• 제26권3호
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• pp.197-206
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• 1988

Klebsiella pneumoniae의 세포외막으로부터 2-furaldehyde를 2-furoic acid로 산화시키는 2-furaldehyde dehydrogenase를 분리하여 그 특성을 조사하였다. 이 효소는 $\beta$-$NAD^{+}$를 특이적으로 요구하였다. 분리과정중의 효소활성도는 2-furaldehyde를 기질로 사용하고 $\beta$-$NAD^{+}$를 조효소로 사용하면서 high performance liquid chromatography에 의해 측정 되었다. 세포외막은 Percoll의 밀도흉배에 의한 초원심분리방법과 $Mg^{2+}$, Triton X-100으로 용해시킨 후, 초원심분리시키는 방법으로 수집되었다. 세포외막단백질은 EDTA와 lysozyme을 처리함으로서 얻어졌고, 효소는 QAE-Sephadex Q-504 S Sephadex G-100-을 사용하면서 column chromatography 방법에 의해 분리되었다. 본 효소는 $85^{\circ}C$, PH9.5, 그리고 1.5% (vol/vol) Triton X-100의 존재하에서 최대활성을 보여주었다. 효소의 분자량은 nondenaturing polyacrylamide gel e electrophoresis의 결과, 88, 000.으로 추정되었고, 2-furaldehyde에 대한 효소의 Km값은 4.72 mM 이였다.

• Journal of Plant Biology
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• 제22권3호
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• pp.55-57
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• 1979

These studies were undertaken to determine the $CO^2$fixation patterns following the chloroplast development in maize leaves. At the early stage of chloroplast development $^{14}C$ was incorporated into aspartate (41%) and malate (22%) respectively. Whereas the incorporation of $^{14}C$ into malate was higher than that of aspartate as chloroplast developed. Activity of NADPH-dependent malate dehydrogenase was increased throughout chloroplast development, but that of aspartate transaminase was not. Much incorporation of $^{14}C$ into aspartate at the early stage of chloroplast development and into malate at later stage of chloroplast development lead us to conclude that NADPH-dependent malate dehydrogenase activity is closely associated with chloroplast development, but activity of aspartate transaminase is not.

• 생약학회지
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• 제20권1호
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• pp.32-36
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• 1989

Effects of Lycium chinensis, Epimedium koreanum and tuguaconitine which is isolated from Aconitum sibiricum on primary culture chicken embryonic brain cells were studied by microscopic observation and determined of the activity of pyruvate dehydrogenase complex(PDHC). Brain cells were prepared from the brain of 10-day-old chicken embryo and cultured with a medicine consisted of 90% Dulbecco's Modified Eagle Medium(DMEM) and 10% horse serum. It was observed that all substances studied seemed to show the tendency to stimulate the neurite outgrowth of brain cells which were cultured with a deficient medium under microscopic observation. The activity of PDHC in brain cells cultured with a deficient medium was increased by Lysium chinensis and Epimedium koreanum. However, tuguaconitine had not influence on the activity of PDHC.

• Applied Biological Chemistry
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• 제42권2호
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• pp.162-165
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• 1999

Spraque-Dawley계 수컷랫트에 단풍취로부터 분리한 화합물을 경구투여하고 혈청 ethanol농도와 간의 ADH 활성에 미치는 효과를 검토한 결과 알코올대사를 촉진시키는 성분은 apigenin $7-O-{\beta}-D-glucoside$로 확인되었다.

• Bulletin of the Korean Chemical Society
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• 제12권5호
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• pp.504-509
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• 1991

S. fradiae showed very high activity of isocitrate dehydrogenase compared to other microorganisms. The activity of this enzyme was increased with the growth of the organism. But the increase might not imply its involvement in the growth. Rather its increased activity seemed to have a connection with the biosynthesis of neomycin. The enzyme showed high specificity toward $NADP^+$ and D-isocitrate with Km values of 5.75 and 6.74 uM, respectively, It was activated by $Mn^{2+}$. Its molecular weight was estimated from its gel retardation coefficient to be in the range of 61,000-63,000 daltons and its optimum pH was 8.0. The enzyme was thermally unstable.

• 생명과학회지
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• 제19권9호
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• pp.1321-1327
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• 2009

본 연구에서는 숙취해소에 좋은 것으로 알려진 식품 소재의 주요 아미노산을 포함하여 효소 활성에 영향을 미치는 것으로 알려진 아미노산을 선택하였고, 효소 활성도가 상대적으로 높은 yeast와 rat liver 유래의 ADH 및 ALDH 효소를 대상으로 알코올 대사에 관련된 효소 활성의 촉진 효과에 대하여 검토하였다. Rat liver 유래의 ADH 활성은 처리한 아미노산 중에서 arginine에서 가장 높았다. Arginine의 첨가 농도를 달리하여 효소 활성을 측정한 결과 $10{\sim}50\;mg$/ml 농도에서 $118{\sim}120.6%$로 양성대조구의 90.6% 보다 약간 높은 것으로 나타났다. 또한, yeast 유래의 ADH 활성은 methionine에서 가장 높은 활성을 보였고, methionine의 처리 농도를 달리한 경우에서는 첨가 농도 의존적으로 높은 활성을 보였다. Rat liver 유래의 ALDH 활성은 methionine이 가장 높은 활성을 보였다. Methionine의 첨가 농도별 측정에서는 10 mg/ml에서 30 및 50 mg/ml 첨가 농도에서 보다 높은 활성을 보였으며, 이들 모든 처리 농도에서 양성대조구 보다 상당히 높은 활성을 보였다. 한편 yeast 유래의 ALDH 활성은 각 아미노산별 큰 차이는 없었으나, arginine에서 높은 활성을 보였다. Arginine의 첨가 농도별 측정에서는 처리 농도 의존적으로 활성이 약간씩 증가하는 경향을 보였으며, 양성대조구 보다 높은 활성을 나타내었다. 효모 유래 ALDH 및 rat liver 유래 ADH 효소 활성을 촉진시키는 작용을 가진 arginine을 효모 배양에 첨가시킬 경우 세포 내 ALDH 및 ADH 활성 염색 정도가 증가함으로써 arginine은 ALDH 및 ADH 활성을 촉진시키는 효능이 in vivo 실험계에서도 확인되었다. 이상의 실험 결과에서 아미노산 중에서는 arginie과 methionine이 ADH 및 ALDH 활성을 촉진시키는 작용에 의해 알코올 분해뿐만 아니라 acetaldehyde의 분해도 촉진시킬 가능성이 높아 숙취해소 효과는 물론 간 보호 효과도 동시에 있을 것으로 시사 되어 진다. 따라서 arginine과 methionine과 같은 아미노산을 주류 제품에 첨가하게 될 경우 숙취해소 경감과 간 보호 효능을 어느 정도 나타낼 수 있을 가능성이 제기되었다.

• Journal of Microbiology and Biotechnology
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• 제18권4호
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• pp.663-669
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• 2008

The solvent-tolerant bacterium Enterobacter sp. VKGH12 is capable of utilizing n-butanol and contains an $NAD^+$-dependent n-butanol dehydrogenase (BDH). The BDH from n-butanol-grown Enterobacter sp. was purified from a cell-free extract (soluble fraction) to near homogeneity using a 3-step procedure. The BDH was purified 15.37-fold with a recovery of only 10.51, and the molecular mass estimated to be 38 kDa. The apparent Michaelis-Menten constant ($K_m$) for the BDH was found to be 4 mM with respect to n-butanol. The BDH also had a broad range of substrate specificity, including primary alcohols, secondary alcohols, and aromatic alcohols, and exhibited an optimal activity at pH 9.0 and $40^{\circ}C$. Among the metal ions studied, $Mg^{2+}$ and $Mn^{2+}$ had no effect, whereas $Cu^{2+},\;Zn^{2+}$, and $Fe^{2+}$ at 1 mM completely inhibited the BDH activity. The BDH activity was not inhibited by PMSF, suggesting that serine is not involved in the catalytic site. The known metal ion chelator EDTA had no effect on the BDH activity. Thus, in addition to its physiological significance, some features of the enzyme, such as its activity at an alkaline pH and broad range of substrate specificity, including primary and secondary alcohols, are attractive for application to the enzymatic conversion of alcohols.

• BMB Reports
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• 제28권2호
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• pp.177-183
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• 1995

The activity of aldehyde dehydrogenase (ALDH) in the cerebrum, cerebellum, striatum, and medulla oblongata was examined and mitochondrial matrix ALDH was purified prior to immunohistochemical study on the localization of ALDH isozymes in pig brain. Relatively high enzyme activity was found in the striatum and medulla oblongata when using indole-3-acetaldehyde as substrate, and in the striatum when using 3,4-dihydroxyphenylacetaldehyde (DOPAL). The main part of mitochondrial ALDH activities with both acetaldehyde and DOPAL existed in the matrix fraction. The ratio of activity of the matrix to the membrane fraction in the cerebrum was higher than in the cerebellum, suggesting that the distribution pattern of ALDH isozymes was different according to the brain regions. The 276-fold purified mitochondrial matrix ALDH from pig brain was identified to be homologous tetramers with 53 KD subunits. The enzyme showed maximal activity at pH 9.0 and was stable in the temperature range from $25^{\circ}C$ to $37^{\circ}C$. The mitochondrial matrix ALDH activity was considerably inhibited by acetaldehyde in vitro. The $K_m$ values of the enzyme for acetaldehyde and propionaldehyde were 5.8 mM and 4.9 mM, respectively, whereas $K_m$ values for indole-3-acetaldehyde and DOPAL were 44 ${\mu}M$ and 1.6 ${\mu}M$, respectively. The $V_{max}/K_{m}$ ratio was the highest with DOPAL as compared with other substrates. These results suggested that mitochondrial matrix ALDH in the present work might be a low Km isozyme involved in biogenic aldehyde oxidation in pig brain.