• Korean Journal of Veterinary Research
• /
• v.29 no.4
• /
• pp.425-431
• /
• 1989

This study was undertaken to investigate the changes of enzyme activities resulted from low concentrated carbon monoxide poisoning on the caudate nucleus in rat. The activities of cytochrome oxidase, succinate dehydrogenase and lactate dehydragenase were observed histochemically, after the experimental animals were poisoned to 100ppm carbon monoxide for 8 hours every day from one day to 16 days. The materials were sliced from coronal section at the level of the optic chiasm and immediately frozen sections of $10{\mu}m$ thickness were cut on the cryostat at $-15^{\circ}C$ and incubated in the medium containing substrate for histochemical detection of cytochrome oxidase, succinate dehydrogenase and lactate dehydrogenase. The sections were mounted in glycerol gelatin and observed under light microscope. It was obtained that cytochrome oxidase activity decreased moderately and succinate dehydrogenase activity showed marked or moderate activity during entire poisoning period and lactate dehydrogenase activity showed marked or moderate activity from one to 8 days but recovered to normal condition at 16th day.

• Korean Journal of Veterinary Research
• /
• v.29 no.4
• /
• pp.461-467
• /
• 1989

The activity of lactate dehydrogenase in plasma and various tissues(skeletal muscle, cardiac muscle, liver, lung, kidney and spleen) of Korean native cattle in a Chonju abattoir, the Breeding Stock Farm and Animal Farm of Chonbuk University was determined by using ultra violet method. Using polyacrylamide gel electrophoresis, the lactate dehydrogenase isoenzyme distrimution of plasma and various tissues in Korean native cattle was studied. The plasma lactate dehydrogenase activity of Korean native cattle was $554.80{\pm}92.70IU/l$ and the lactate dehydrogenase activity of male plasma was $543.96{\pm}97.89IU/l$, which was lower than that of female plasma, $579.19{\pm}78.09IU/l$. The plasma lactate dehydrogenase activity of calf was $557.31{\pm}110.27IU/l$ and was no significantly different from that of adult Korean native cattle. But the range of calf lactate dehydrogenase activity was larger than that of adult Korean native cattle. In tissues, the lactate dehydrogenase activity was decreased in order of lung, kidney, spleen, liver, heart and skeletal muscle. The lung had the greatest activity and the skeletal muscle had the least. Lactate dehydrogenase isoenzymes in plasma and tissues were found to have a characteristic distribution and quantitative isoenzyme patterns. In plasma, the LDH1 usually had the greatest activity and other isoenzymes showed a decreasing tendency in order of LDH2, LDH3, LDH4 and LDH5. The distribution of lactate dehydrogenase isoenzymes had a wide variation in tissues. But the distribution of LDH isoenzymes in plasma was similar to that in kidney, and also cardiac muscle and spleen had similar pattern in LDH isoenzymes distribution.

• YAKHAK HOEJI
• /
• v.32 no.6
• /
• pp.377-385
• /
• 1988

The biologically active component of licoris(Glycyrrhizae Radix L.) is considered to be glycyrrhetinic acid, an aglycone of glycyrrhizin, on the basis of chemical and pharmacological studies. The present study was undertaken to investigate the effect of glycyrrhetinic acid on the hepatic morphine-6-dehydrogenase activity, which catalize morphine to morphinone. Morphine-6-dehydrogenase was further purified by centrifugation, $(NH_4)_2SO_4$ fractionation, sephadex G-100, hydroxyapatite column. Hepatic morphine-6-dehydrogenase activity was significantly decreased by the treatment of glycyrrhetinic acid. When effect of glycyrrhetinic acid on the hepatic morphine-6-dehydrogenase was investigated in vitro, it was powerfully inhibited the enzyme activity with dose-dependent manner. From the above results, glycyrrhetinic acid inhibits hepatic morphine-6-dehydrogenase activity and decreases the morphine induced harmful side effects.

• Nutrition Research and Practice
• /
• v.2 no.4
• /
• pp.195-199
• /
• 2008

Alcoholism has been associated with folate deficiency in humans and laboratory animals. Previous study showed that ethanol feeding reduces the dehydrogenase and hydrolase activity of 10-formyltetrahydrofolate dehydrogenase (FDH) in rat liver. Hepatic ethanol metabolism generates acetaldehyde and acetate. The mechanisms by which ethanol and its metabolites produce toxicity within the liver cells are unknown. We purified FDH from rat liver and investigated the effect of ethanol, acetaldehyde and acetate on the enzyme in vitro. Hepatic FDH activity was not reduced by ethanol or acetate directly. However, acetaldehyde was observed to reduce the dehydrogenase activity of FDH in a dose- and time-dependent manner with an apparent $IC_{50}$ of 4 mM, while the hydrolase activity of FDH was not affected by acetaldehyde in vitro. These results suggest that the inhibition of hepatic FDH dehydrogenase activity induced by acetadehyde may play a role in ethanol toxicity.

• Korean Journal of Microbiology
• /
• v.24 no.4
• /
• pp.370-376
• /
• 1986

From the outer membrane portion of Gram-negative Klebsiella pneumoniae, the activity of 2-furaldehyde dehydrogenase depending upon beta-nicotinamide adenine dinucleotide was detected. Cytoplasmic membrane was preferentially extracted from crude membrane with $Mg^{2+}$ and Triton X-100, and then outer membrane was collected by ultracentrifugation. The crude enzyme was obtained by solubilization of outer membrane with lysozyme, ethylene diamine tetraacetate and Triton X-100. Thereafter 2-furaldehyde dehydrogenase was partially purified through column chromatography on QAE-Sephadex Q-50 and Sephadex G-150 and the enzyme activity was analyzed by means of high performance liquid chromatography. The optimal pH for the activity of the enzyme was about 9.5 and the optimal temperature was about $85^{\circ}C$. The partially purified enzyme retained tis activity at $85^{\circ}C$ for 5 hours. The optimal concentration of Triton X-100 for the activity of the enzyme was about 1.5% in the reaction mixture.

• Microbiology and Biotechnology Letters
• /
• v.27 no.2
• /
• pp.124-128
• /
• 1999

TK6 was able to produce NAD+ dependent cyclohexanol dehydrogenase(CDH). The production of CDH was increased rapidly at the logarithmic phase and maintained constantly after that. In order to investigate the inductive production of CDH by various substrates, the bacteria were grown in the media containing alicyclic hydrocarbons and various alcohols as a sole crabon souce. CDH was induced most actively by cyclohexanol. Cyclohexanone and cyclohexane-1,2-diol also induced remarkable amount of CDH but it was induced weakly by 1-propanol, 1-butanol, 1-pentanol, 1-hexanol, 2-propanol, and 2-methyl-1-propanol. The dehydrogenase of the bacteria grown in the media containing cyclohexanol were weakly active for various alcohols, but the dehydrogenase activity for cyclohexane-1,2-diol was twice as much as that for cyclohexanol. Activity staining on PAGE of the cell free extract of Rhodococcus sp. TK6 grown in the media containing cyclohexanol reveals at least sever isozyme bands of CDH and we nominated the four major activity bands as CDH I, II, III, and IV. CDH I was strongly induced by cyclohexanol, cyclohexane-1,2-diok, but its activity was specific to cyclohexane-1,2-diol and 1-pentanol. CDH IV was strongly induced by cyclohexanol and cyclohexane-1,2-diol, and its activity was very specific to cyclohexane-1,2-diol.

• Archives of Pharmacal Research
• /
• v.26 no.3
• /
• pp.197-201
• /
• 2003

Novel $\beta$-hydroxy propenamides as analogues of the active metabolite of leflunomide (A 771726) were synthesized and evaluated for their inhibitory activity on dihydroorotate dehydrogenase (DHODH) in an investigation into their immunosuppressive activity. Compounds 2a, 3a, and 3h were approximately 4-40 times more potent than leflunomide in their activity while they were-less active than A 771726.

• The Korean Journal of Food And Nutrition
• /
• v.25 no.4
• /
• pp.747-754
• /
• 2012

The objective of this study was to investigate free amino acid composition, antioxidant activity, alcohol dehydrogenase activity and the sensory quality attributes for the development of functional soy sauce using Hutgae (Hovenia dulcis Thunb) fruit, which is well-known for improving liver function and alleviating various negative physiological effects following heavy consumption of alcoholic beverages. Soy sauces adding six types of extract from Hutgae fruit (HF) were prepared (SSH1: HF 20%, SSH2: HF 10%, SSH3: HF 20%/40 days NaCl extract, SSH4: HF 20%/20 days NaCl extract, SSH5: HF 20% water bath extract, SSH6: freeze-drying powder from HF 20% aqueous extract), compared with soy sauce using the conventional method. These soy sauces were used for determining alcohol dehydrogenase activity by NADH absorbance, the antioxidant effect by 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity and sensory evaluation by sensory scaling. Total free amino acid contents for most samples were in the range of 327.3 to 375.5 mg%, and then, aspartic acid and glutamic acid content of SSH1 and SSH5 were higher than that of others. DPPH radical scavenging activity was shown to be the highest in SSH4, also SSH1, SSH5 and SSF6 were shown to be higher than the control group. Alcohol dehydrogenase activity was shown to be the highest in SSH5. In sensory evaluation, the highest intensity of roast smell was observed in SSH4 while sweet taste was shown to be the highest in SSH5, and SSH3 and SSH5 revealed higher overall acceptability. From these results, Hutgae fruit soy sauces demonstrated antioxidant activity and alcohol dehydrogenase activity. In conclusion, soy sauces containing the water bath extract of Hutgae fruit may be used as a functional seasoning.

• Korean Journal of Soil Science and Fertilizer
• /
• v.40 no.4
• /
• pp.229-233
• /
• 2007

A long-term rice paddy field, which is located in the National Institute of Crop Science (Suwon city, Korea) has been managed for studying of fertilization and composting impact on paddy soil fertility since 1954. The objective of this research was to evaluate soil quality through dehydrogenase analysis in long-term paddy soil treatment plots, such as control, N fertilization (N), NPK fertilization (NPK), and rice straw compost with NPK (CNPK). Dehydrogenase-producing bacterial population developing red-colored triphenyl formazan (TPF) was highly correlated to the dehydrogenase activity in rice paddy soils sampled prior to waterlog. The dehydrogenase-producing bacterial population and dehydrogenase activity was comparatively high in plots of NPK, and CNPK, which organic matter content was relatively high.

• BMB Reports
• /
• v.28 no.5
• /
• pp.408-413
• /
• 1995

Decrease in the amount of cotyledonary spermidine in Glycine max under anaerobic conditions related to an increase in spermidine dehydrogenase. Under the same conditions, no enzymatic activity of diamine oxidase was observed. Exposure of Glycine max both to spermidine and 1,3-diaminopropane under anaerobic conditions resulted in a decrease in spermidine contents. Correlated with the decrease in spermidine contents, there was a drastic increase in spermidine dehydrogenase. The molecular weight of the purified enzyme estimated by Sephacryl S-300 gel column and SDS gel electrophoresis were 130,000 dalton and 65,000 dalton, respectively, indicating that the enzyme is a dimer. The optimal pH for activity was 9.3. The $K_m$ value for spermidine was 0.61 mM. Neither metal ions nor polyamine and derivatives affected enzymatic activity, but the enzyme was inhibited by DTNB, NEM and PCMB, suggesting that a cysteine residue of the enzyme is associated with or involved in enzyme activity. To our knowledge, this is the first report describing properties of the enzyme from plants. Considered together, the data in this paper indicate that both spermidine and 1,3-diaminopropane, novel activators, enhance the spermidine dehydrogenase activity and control the intracellular spermidine contents.