• Journal of Life Science
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• v.19 no.2
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• pp.256-263
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• 2009

The lactate dehydrogenase (EC 1.1.1.27, LDH) $A_4$ isozyme in skeletal muscle of mandrin fish (Siniperca scherzeri) was successfully purified by affinity chromatography and ultrafiltration. The molecular weight of the purified LDH $A_4$ isozyme was 140.4 kDa and its isoelectric point (pI) was 7.0. Optimal pH for enzymatic reaction was 7.5. ${K_m}^{PYR}$ and $V_{max}$ value of the purified LDH $A_4$ isozyme were $4.86{\times}10^{-5}$ M and 13.31 mM/min using pyruvate as a substrate, respectively. These kinetic properties of the purified LDH $A_4$ isozyme supported the fact that the mandrin fish was a warm-adapted species. The antibody against the purified LDH $A_4$ isozyme may be used in the metabolic physiological studies of ectothermic vertebrates and in the diagnosis of several human diseases.

• Journal of Life Science
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• v.15 no.1 s.68
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• pp.71-79
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• 2005

The metabolism of lactate dehydrogenase (EC 1.1.1.27, LDH) and $C_4$ isozyme were studied in tissues of Coreoperca herzi and Pseudogobio esocinus acclimated to rapid increase of dissolved oxygen (DO). In C. herzi the LDH activity was changed $35-39\%$ in brain and liver tissues, and within $20\%$ in other tissues. The $B_4$ isozyme was increased and isozyme containing subunit C was decreased in muscle tissue. The $B_4$ isozyme was increased in heart and kidney. In P. esocinus, the LDH activity in liver tissues was largely increased to $150\%$ for 30 minute and $70\%$ in other tissues. The $A_4$ isozyme was increased in muscle and $B_4$ isozyme was increased in other tissues. Especially, the metabolism of liver tissue in P. esocinus was regulated by increasing liver-specific $C_4$ and decreasing $A_4$ isozyme. But the metabolism of eye tissue in C. herzi was regulated by decreasing LDH activity and eye-specific $C_4$ isozyme. The LDH activity and LDH isozyme in P. esocinus were largely increased than C. herzi acclimated to rapid increase of DO. And eye-specific $C_4$ and liver-specific $C_4$ isozymes played role as lactate oxidase. Therefore, the response of species acclimated to rapid increase of DO seems to be variable, perhaps due to prior exposure to environmental conditions.

• 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.

• Korean Journal of Food Science and Technology
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• v.37 no.1
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• pp.95-102
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• 2005

Effects of Morus alba fruit extracts on monoamine oxidase (MAO) activity were examined in rats during and after physical exercise. Oral administration of M. alba extract (0.3 g/kg body weight) significantly increased brain MAO-A activity but decreased liver MAO-B activity when they were measured using serotonin and benzylamine as substrates. Type of physical exercises had significant effect on MAO activity. Brain MAO-A activity markedly decreased with physical activity-related stress compared to normal group, whereas Liver MAO-B activity increased up to 60 min after exercise. Lactate dehydrogenase (LDH) activity and lactate concentration in blood, clinical indices of physical exercise activities, were also determined for correlation to MAO activities. MAO-A activity of rats subjected to oral administration of M. alba extract and physical exercise increased whereas MAO-B and LDH activities, and lactate level decreased, All indices eventually recovered normal levels, These results suggest M. alba may increase capability of physical activities by modulating MAO activities during exercise.

• Journal of Life Science
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• v.20 no.3
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• pp.416-423
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• 2010

In this study, the properties and gene expression of the lactate dehydrogenase (EC 1.1.1.27, LDH) isozyme were studied in angelfish (Pterophyllum scalare) - known for their adaptation to the low oxygen environment of the tropics - which were acclimated to acute temperature change ($27{\pm}0.5{\rightarrow}18{\pm}0.5^{\circ}C$) and dissolved oxygen (DO) change ($6{\pm}1{\rightarrow}18\;ppm$) for 2 hours. The properties of the LDH isozymes were confirmed in the native-polyacrylamide gel electrophoresis, Western blot analysis and enzyme activity measurement. Liver- and eye-specific Ldh-C gene were expressed in liver, eye and brain tissues. Through Western blot analysis, the LDH $A_4$ isozyme was shown to have a more cathodal mobility relative to the $B_4$ isozyme. In the liver tissue, the LDH $A_4$ isozyme increased with temperature drop while the $B_4$ isozyme decreased. The LDH $A_4$ and $C_4$ isozymes increased with DO increment, while the $B_4$ isozyme decreased. In the eye tissue, the LDH $A_4$ and B4 isozymse increased with temperature drop while the $B_4$ isozyme decreased. The LDH $A_4$ and $B_4$ isozymes increased with DO increment, but the $C_4$ isozyme and isozymes including the subunit C decreased. In the heart tissue, LDH activity increased with DO increment, as well as the LDH $B_4$ isozyme. In the brain tissue, the LDH $A_4$ and $B_4$ isozymes increased with temperature drop. The LDH $B_4$ isozyme increased with DO increment. Accordingly, since the liver- and eye-specific Ldh-C are influenced by changes in DO and the LDH $B_4$ and $C_4$ isozymes are relatively controlled in the liver and eye tissues, the $C_4$ isozyme can be considered to have a lactate oxidase function.

• The Korean Journal of Zoology
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• v.22 no.1
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• pp.1-10
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• 1979

From the experimental results of cellulose acetate membrane electrophoresis we concluded the followings in explaining the LDH isozyme patterns found in the retina and cerebrum of vertebrata. Lactate dehydrogenase of the retina and cerebrum of both Carassinus carassinus and Cyprinus carpio was found to have one diffused band located between $LDH_2$ and $LDH_1$. LDH isozyme patterns of heart, pectoral muscle, liver and stomach of the Cyprinus carpio had the same diffused band in all organs. LDH isozyme patterns of the cerebrum of Hynobius leechii and Rana nigromaculata were observed to be different, in Hynobius leeichi a single band moved to the negative pole and two bands of $LDH_5$ and $LDH_4$ were obtained in the Rana nigromaculata. The retina and cerebrum of Natrix tigrina lateralis were observed as one band but amyda maakii had different LDH isozymes of the retina and cerebrum. The retina of Amyda maakii had five distinct LDH isozyme bands which had decreasing activity in the order of $LDH_5, LDH_4, LDH_3, LDH_2 and LDH_1$. The cerebrum of Amyda maakii had one band like Natrix tigrina lateralis but it moved to the negative pole. LDH isozymes in the retina and cerebrum of Gallus gallus domesticus and Melopsittacus undulatus showed one band. Five characteristic LDH isozyme bands were obtained from the retina of mammals, Oryctolagus cuniclus, Canis familiaris, Sus scrofa bos taurus and in the cerebrum of mouse, albino rat, Rhinolophus ferrum-equinum kokai.

• YAKHAK HOEJI
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• v.32 no.4
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• pp.239-244
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• 1988

Transcriptional rate of lactate dehydrogenase A-gene(LDH-A) during the prereplicative phase of regenerating rat liver was determined by in vitro run-off transcription assay. The results show that the transcription rate of LDH A-gene increases between 12 hours and 15 hours peaking at 13 hours after partial hepatectomy of rat liver. The increased rate of LDH A-gene transcription was interfered after DL-propranolol treatment intraperitoneally injected twice at 1 hour and 8 hours after partial hepatectomy indicating that the transcriptional control of LDH A-gene expression may be mediated by beta adrenergic receptor and cAMP as a second messenger. And also was it shown that the temporally increased rate of LDH A-gene transcription was maximum one hour after the second cAMP-surge which is known to play an important role for the initiation of DNA replication during regeneration of rat liver. And the transcriptional rate of LDH A-gene was decreased to the basal level at the time period when the hepatocytes proliferate rapidly suggesting that the induced LDH Aisozyme may be required for the initiation of DNA replication during regeneration of rat liver. These data may be supporting for the hypothesis suggesting that the induced LDH A-isozyme during the pre-replicative phase of regenerating rat liver may play bifunctional roles as a glycolytic enzyme and a helix destablizing protein as well.

• Journal of Microbiology and Biotechnology
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• v.12 no.5
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• pp.716-721
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• 2002

The ldhL gene encoding the $_L$-(+) lactate dehydrogenase was cloned from Lactobacillus reuteri ATCC 55739 chromosomal DNA and characterized. An internal 750-bp fiagment of ldhL gene was amplified by PCR using primers based on the conserved region of lactobacilli ldhL genes. A genomic library off. reuteri ATCC 55739 was constructed using pBR322, and colony hybridization experiments were performed using the 750-bp fragment as aprobe. One clone harboring a 4.0-kb PstI fragment was identified, and nucleotide sequencing confirmed it as an open reading frame of 972 bp in size in the middle. In addition to IdhL gene, an ORF homologous to Streptococcus pneumoniae TIGR4 hydrolase gene and 3' part of phosphomevalonate kinase gene (mvaK2) were also found on the 4 kb fragment. $_L$-LDH of L. reuteri ATCC 55739 showed the highest degree of homology with the $_L$-LDH of Pediococcus acidilactici (62.4%), fullowed by the $_L$-LDH of Lactobacillus pentosus (58.7%). The size of IdhL transcript determined by Northern blot was 1 kb, indicating the monocistronic nature of IdhL.

• Korean Journal of Microbiology
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• v.15 no.3
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• pp.103-112
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• 1977

Several strains of spore-forming lacticacid bacteria were isolated from natural sources such as soils, cereals, and foods. The general morphological and physiological characteristics of the strain 6-4 were investigated nad compared with some other industrial strains. The effects of fructose-1,6-diphoshpate (FDP), adenosine triphosphate (ATP), and pH on the lactate dehydrogenase(LDH) activity of the strain were studied, and the changes in LDH activity and spore formation under various cultural conditions were researched. The results were as follows. 1. This strain was identified to Bacillus coagulans Hammer and distributed widely in natural sources. 2. The strain strongly converted various fermentation substrates in to L(+)-lacticacid in anaerobic conditioins, and many spores that were of great advantages to the industrial application were formed easily in the aerobic condition. 3. The LDH activity of this strain was activated by FDP and inhibited by ATP. The optimal pH for the enzyme activity was 6.0-6.5. 4. In the anaerobic culture condifion, the large amount of glucose added in the medium increased the LDH activity, but the cells were not committed to sporulate. 5. When none or a very small amount of glucose (less than 0.5%) was added to culture medium in the aerobic condition, the LDH activity was decreased and many spore were produced with final pH higher than 8.5. 6. The additioin of large amount of glucose (more than 2.0%) in aerobic culture increased the LDH activity and inhibited strongly the spore formation with final pH lower than 6.0.

• The Korean Journal of Zoology
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• v.16 no.3
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• pp.193-201
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• 1973

A cellulose acetate electrophoretic survey of Korean Anura has revealed the presence of diverse lactate and malate dehydrogenase isozymes. The LDH and MDH isozymes in the tissues of the brain, heart, stomach, skeletal muscle and liver of the six species of Anura examined show the species specific patterns which differ from those of mammals and birds. Two isozymic forms of LDH and MDH exist in both Rana nigromaculata and Rana nigromaculata coreana, respectively, with almost the same pattern. LDH of Bombina orientalis has five isozymic forms, and that of Rana temporaria ornativentris contains four isozymes. Bufo sp. has 3 to 5, and Rana rugosa has 3 to 4 isozymic bands according to the tissues. MDH's of all animals have two isozymic forms with different spacing on the zymograms.