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

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

• YAKHAK HOEJI
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• v.38 no.4
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• pp.401-409
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• 1994

The cholinergic activity of dammarane glycosides of Panax ginseng was examined both morphologically and chemically on primary cultures of chicken embryonic brain cells. When primary cultured chicken embryonic cells were treated with $50\;{\mu}g/ml$ of total dammarane glycosides of Panax ginseng followed by the exposure to 10mM atropine for 48 hr, lactate dehydrogenase levels within the cells remained at 36% of untreated control values while atropine-treated controls fell to 0% lactate dehydrogenase. It was found that cholinergic activity was mainly exerted by the panaxadiol glycosides. The treatment of the cells with $50\;{\mu}g/ml$ of panaxadiol glycosides followed by the exposure to atropine, lactate dehydrogenase levels within the cells remained at 60% of untreated control values. Ginsenoside $Rb_1$, a component of panaxadiol glycosides, was found to exert the cholinergic activity keeping the lactate dehydrogenase levels within the cells at 70% of untreated control values. The cholinergic activity of ginsenoside $Rb_1$ seems to be exerted through acting on the $Ca^{2+}$ channel in cultured brain cells.

• Journal of Physiology & Pathology in Korean Medicine
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• v.20 no.1
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• pp.25-30
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• 2006

This Study was designed to investigate the effects of Patholobi Caulis on the change of regional cerebral blood flow (rCBF) and blood Pressure (MABP) in normal and Cerebral ischemic rats. And, this Study was designed to investigate the inhibition of lactate dehydrogenase (LDH) activity in neuronal cells. The results were as follows : In normal rats, Patholobi Caulis significantly increased rCBF in a dose-dependent manner, and MABP was somewhat increased. In ischemia rats, rCBF was significantly and stably increased by Patholobi Caulis (10 mg/kg, i.p.) during the period of cerebral reperfusion, which contrasted with the findings of rapid and marked increase in control group. Patholobi Caulis significantly inhibited LDH activity in neuronal cells. It was suggested that Patholobi Caulis had an anti-ischemic effect through the improvement of cerebral hemodynamics and inhibitive effect on the brain damage.

• Preventive Nutrition and Food Science
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• v.8 no.3
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• pp.265-269
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• 2003

Gamma irradiation treatment was performed at the early and mid-fermentation stages of Kimchi preparation. Changes in fermentative microorganisms and lactate dehydrogenase activity during the fermentation periods were investigated to determine proper irradiation point for extending the shelf life of Kimchi. Initial levels of acid producing bacteria and yeast in Kimchi were 10$^4$ CFU g$^{-1}$ and 10$^1$ CFU g$^{-1}$ , and reached up to 10$^{9}$ CFU g$^{-1}$ after 15 days and 10$^{7}$ CFU g$^{-1}$ after fermentation for 30 days at 1$0^{\circ}C$, respectively. The radiation resistance of acid producing bacteria in the earlier stage (D$_{10}$ value was 0.87 kGy) was higher than at the midfermentation stage (after 10 days at 1$0^{\circ}C$, D$_{10}$ value was 0.69 kGy). Microbial growth and lactate dehydrogenase activity were inhibited significantly by gamma irradiation at the early fermentation stage of Kimchi and acidification was effectively delayed during the subsequent storage period. Although the growth of fermentative microorganisms was inhibited by gamma irradiation at the mid-fermentation stage of Kimchi, lactate dehydrogenase activity was maintained and acidification continued during the storage period.

• Asian-Australasian Journal of Animal Sciences
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• v.17 no.10
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• pp.1411-1416
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• 2004

The objective of this work was to isolate a microorganism, able to produce high lactate dehydrogenase (LDH) activity, for use as a microbial feed additive. The LDH is an important enzyme for lactate conversion in the rumen, thereby possibly overcoming lactic acidosis owing to sudden increases of cereal in the diets of ruminants. In the present study, various bacterial strains were screened from a variety of environments. Among the isolated microorganisms, strain FFy 111-1 isolated from a Korean traditional fermented vegetable food called Kimchi showed the highest enzyme activity, along with retaining strong enzyme activity even in rumen fluid in vitro. Based on morphological and biochemical characteristics as well as compositions of cellular fatty acids plus API analyses, this strain was identified as Lactobacillus sp. The optimum temperature and pH for growth were found to be 30$^{\circ}C$ and pH 6.5, respectively. A maximum cell growth of 2.2 at $A_{650}$ together with LDH activity of 2.08 U per mL was achieved after 24 h of incubation. Initial characterization of FFy 111-1 suggested that it could be a potential candidate for use as a direct-fed microbial in the ruminant animals.

• Journal of Periodontal and Implant Science
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• v.16 no.1
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• pp.93.1-93.1
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• 1986

• Environmental Analysis Health and Toxicology
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• v.10 no.1_2
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• pp.15-20
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• 1995

The effects of volatile substances inhalation on lactate dehydrogenase and cholinesterase in rats were investigated. Male Sprague-Dawley rats were exposed to marketed odorant, ethyl acetate and ethyl ether for 15 days. Enzyme activities were measured in serum and several tissues such as liver, lung, brain, heart, kidney and muscle to find differences of effects according to the organ. Cholinesterase activity in serum and most of tissues revealed time-dependent decrease in the case of marketed odorant inhalation. Especially in heart and kidney significant decrease was observed. Ethyl acetate exposure to rats revealed also decrease in serum and all tissues by 40% to 60%. Ethyl ether inhalation showed significant decrease by 30% to 50%. Lactate dehydrogenase activity was markedly increased in serum and similarly in heart, brain and kidney by exposure to marketed odorant. No changes were observed in liver. Ethyl acetate exposure to rats revealed increase in serum by about 200%, compared to normal group and in other tissues by 40% to 70% except in liver and muscle. Ethyl ether inhalation showed significant increase in serum by about 100%. There was no change in 'liver and slight increase in muscle.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.6
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• pp.964-972
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• 1994

The 4.3-kb gene coding for L-lactate dehydrogenase of Bacillus stearothermophilus has been subcloned and expressed in E. coli cells. The enzyme was purified 200-fold with 25% yield by heat treatment , DEAE-Sephadex, and NAD++ -Sepharose CL-4B affinity chromatography followed by gel filtration through Sephadex G-200 . The molecular weight of the purfied enzyme was estimated to be about 35, 000 and 140, 000 on SDS-polyacrylamide gel electrophoresis and gel filtration, respectively. indicating that the enzyme is composed of four identical subunits. THe enzyme for pyruvate reduction and lactate oxdiation was stable at 60 and 75$^{\circ}C$ for 30 min, and the optimal temperatures for both reactions were 60 and 7$0^{\circ}C$, respectively. The enzyme had an optimal pH at 5.5 and 8.5 in pyruvate reduction and lactate oxidation, respectively. The pH stability of enzyme of pyruvate reduction was table between pH 5 and 7. more than 90% of enzyme activity was lost at 1mM FeSO4 and p-chloromercuribonzoate. The maximal activation of the enzyme was obtained with 0.8mM fructose 1, 6-bisphosphate.

• YAKHAK HOEJI
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• v.16 no.1
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• pp.34-46
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• 1972

Lactate dehydrogenase isozymes in heart, kidney, liver and skeletal muscle of 15 species of vertebrate animals belonging to 5 classes were separated by cellulose acetate electrophoresis and the levels of them were measured and compared with each other. Lactate dehydrogenase isozyme patterns were different from each other among animal species and among tissues. The activity of LDH$_{5}$ was superior in anaerobic tissues such as liver and skeletal muscle, and the activity of LDH$_{1}$ was superior in aerobic tissues such as heart and kidney. The level of LDH of vertebrate animals of the 5 classes has found approximatry increasing in the following order: Pisces>Amphibia>Reptelia