• 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 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.

• International Journal of Industrial Entomology and Biomaterials
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• v.18 no.2
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• pp.91-95
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• 2009

The presence of considerable amount of enzymes of TCA cycle isocitrate dehydrogenase (ICDH-NADP+, EC1.1.1.42), $\alpha$-ketogluterate dehydrogenase ($\alpha$-KGD, EC1.2.4.2) and malate dehydrogenase (MDH, EC1.1.1.37) in fresh control and in vitro starved adult Isoparorchis hypselobagri establish the functional TCA cycle in this fluke. The major metabolic end products are pyruvate, lactate, oxaloacetate and malate. The ratio of oxaloacetate/malate assess that oxaloacetate is reduced to malate and in this fluke the reverse TCA cycle is active. The pyruvate/lactate ratio shows pyruvate is reduced to lactate and the fluke is homolactate farmenters.

• The Korean Journal of Zoology
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• v.15 no.4
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• pp.193-205
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• 1972

Lactate and malate dehydrogenase isozymes in crude extracts of various tissues from 28 avian species were investigated by means of celluose acetate electrophoresis. In a given species the presence of two types of the malate dehydrogenase isozymes could be revealed in somatic tissues; one was characterized by fast electrophoretic mobility, and the other by slow mobility. Although the bird lactate dehydrogenase isozymes existed in a variety of species-specific molecular forms, they seemed to show the same pattern within the same genus and family.

• 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

• KSBB Journal
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• v.11 no.4
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• pp.489-496
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• 1996

Metal dispersed carbon paste electrodes were fabricated, and their electrochemical properties were investigated. Among various metal dispersed carbons, platinum-dispersed carbon paste electrode showed most efficient electrocatalytic characteristics. The overpotential for the oxidation of NADH was significantly lowered in the platinum-dispersed carbon paste electrode, and catalytic current was also enhanced. Based on these electrocatalytic observations, L-lactate biosensor using L-lactate dehydrogenase was constructed to evaluate its performance in terms of sensitivity and stability.

• Journal of Yeungnam Medical Science
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• v.12 no.1
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• pp.48-55
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• 1995

The present study was designed to evaluate the efficiency of total lactate dehydrogenase, total creatine kinase, LD1/LD2 ratio, CK-MB and newly developed troponin T in acute myocardial infarction. The level of troponin T was $0.01{\pm}0.02{\mu}g/L$ in 34 healthy person, but the peak vaule of acute myocardial infarction ranged in 4.7-24.2 ${\mu}g/L$. Total lactate dehydrogenase was peaked in 1 to 3 days after chest pain and then progressively decreased, but LD1/LD2 ratio was persistently higher than 1.0 for 10 days in most patients. Total creatine kinase and CK-MB were peaked in 1-2 days, and normalized in 3-4 days, so they were useful in early diagnosis of acute myocardial infarction, but not for the late stages of acute myocardial infarction. Troponin T is early elevated and persistently high level for more than 10 days. Comparing with total lactate dehydrogenase, total creatine kinase, LD1/LD2 ratio and CK-MB, troponin-T test improves the efficiency of serodiagnostic method for the detection of ischemic myocardial damage.

• 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.