• 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.

• Biotechnology and Bioprocess Engineering:BBE
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• v.9 no.4
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• pp.318-322
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• 2004

Lactic acid is an environmentally benign organic acid that could be used as a raw material for biodegradable plastics if it can be inexpensively produced by fermentation. Two genes (ldhL and ldhD) encoding the L-(+) and D-(-) lactate dehydrogenases (L-LDH and D-LDH) were cloned from Lactobacillus sp., RKY2, which is a lactic acid hyper-producing bacterium isolated from Kimchi. Open reading frames of ldhL for and ldhD for the L and D-LDH genes were 962 and 998 bp, respectively. Both the L(+)- and D(-)-LDH proteins showed the highest degree of homology with the L- and D-lactate dehydrogenase genes of Lactobacillus plantarum. The conserved residues in the catalytic activity and substrate binding of both LDHs were identified in both enzymes.

• Journal of Veterinary Clinics
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• v.18 no.4
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• pp.380-389
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• 2001

Non-human primates have been increasing in demand as important experimental animals and companion animals, domestically and internationally. The number of non-human primates for these purposes will be much enhanced in the near future. Despite this trend, basic physiological data are scarcely available in these animal species, leading to the difficulty to diagnose diseases when necessary, due to the absence of reference values. Particularly, there is not any report on the total activity of LDH of non-human primates, let alone LDH isoenzyme patterns, in Korea. LDH isoenzymes have a high level of efficaciousness as diagnostic and prognostic aids in various diseases. In this study, total activities and isoenzyme patterns of LDH were measured to obtain their reference values in domestically reared common marmosets, crab-eating macaques and Japanese macaques. There were widespread different values of serum total LDH among the non-human primate species experimented in this study. Serum LDH values of common marmosets and crab-eating macaques were 597.5$\pm$243.1 IU/l and 605.3$\pm$312.6 IU/l, respectively, whereas those of Japanese macaque showed 1,209$\pm$473.8 IU/l. Five isoenzyme fractions of LDH were observed in all experimented non-human primates but their ranks and proportions represented different patterns one another. In common marmosets, the percent of fraction for serum LDH1, LDH$_2$, LDH$_3$, LDH$_4$, and LDH$_{5}$ was 13.7$\pm$6.4%, 23.3$\pm$3.6%, 29.2$\pm$5.0%, 9.4$\pm$1.4% and 24.4$\pm$7.5%, respectively. The rank of LDH isoenzymes was LDH$_3$>LDH$_{5}$>LDH$_2$>LDH$_1$>LDH$_4$, in the descending order. For crab-eating macaques, the fraction of serum LDH$_1$, LDH$_2$, LDH$_3$, LDH$_4$, and LDH$_{5}$ occupied 19.5$\pm$12.7%, 25.3$\pm$9.3%, 23.8$\pm$8.1%, 10.2$\pm$2.8% and 21.3$\pm$14.2%, respectively. The order of LDH isoenzymes was LDH$_2$>LDH$_3$>LDH$_{5}$>LDH$_1$>LDH$_4$, from top to down. On the while, in Japanese macaques, the fraction of serum LDH$_1$ to LDH$_{5}$ showed 23.4$\pm$11.8%, 30.5$\pm$4.1%, 17.4$\pm$3.9%, 11.3$\pm$3.7% and 13.8$\pm$5.6%, respectively. The decreasing order indicated LDH$_2$>LDH$_1$>LDH$_3$>LDH$_{5}$>LDH$_4$. In conclusion, values such as LDH and LDH isoenzyme patterns of investigated for the first time from non-human primates reaared in Korea, could be reference values for the optimal diagnosis and therapy of diseases of the corresponding animal species. Other parameters of hematology and blood biochemistry are urgently needed to study for the benefit of our intimate non-human primates.an primates.

• Journal of Korean Medicine Rehabilitation
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• v.28 no.4
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• pp.43-50
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• 2018

Objectives Upper lumbar disc herniation (LDH) (L1/2, L2/3) has specific anatomical characteristics and different outcome after conventional treatment compared to lower LDH (L3/4, L4/5, L5/S1). The purpose of this study was to compare the clinical features and effects of korean medical treatment of upper LDH between lower LDH. Methods We retrospectively reviewed the clinical data collected from 121 patients who was had admitted at the Haeundae Jaseng Hospital of Korean Medicine from June 1st, 2014 to August 31th, 2018. The patients who had treated at L1/2, L2/3 level LDH were grouped and compared with those treated at the L3/4, L4/5, L5/S1 level. We reviewed the patient characteristics such as age, the positive rate of Straight Leg Raise Test (SLR test), the presence or absence of previous lumbar surgery. Numeric Rating Scale (NRS) and Oswestry Disability Index (ODI) were evaluated at adimission and discharge. Results Mean age was significantly higher at upper LDH group and positive rate of SLR test was higher at lower LDH group. There was no significant difference of gender and previous lumbar surgery between two groups. Each group had a significant improvement of NRS, ODI scores. But between two groups, there was no significant difference of NRS, ODI scores. Conclusions Upper LDH group was older than lower LDH group. SLR test was useful tool to exclude upper LDH. Korean medical treatment was significantly effective to both upper and lower LDH groups. Further well designed prospective comparative studies are needed.

• Journal of Microbiology and Biotechnology
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• v.25 no.1
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• pp.81-88
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• 2015

This study describes a novel strategy to regulate the metabolic flux for lactic acid production in Lactobacillus casei. The ldhL gene encoding _L-lactate dehydrogenase (L-LDH) was overexpressed in L. casei, and a two-stage oxygen supply strategy (TOS) that maintained a medium oxygen supply level during the early fermentation phase, and a low oxygen supply level in the later phase was carried out. As a consequence, a maximum L-LDH activity of 95.6 U/ml was obtained in the recombinant strain, which was over 4-fold higher than that of the initial strain. Under the TOS for L. casei (pMG-ldhL), the maximum lactic acid concentration of 159.6 g/l was obtained in 36 h, corresponding to a 62.8% increase. The results presented here provide a novel way to regulate the metabolic flux of L. casei for lactic acid production in different fermentation stages, which is available to enhance organic acid production in other strains.

• Korean Journal of Microbiology
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• v.46 no.2
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• pp.213-218
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• 2010

Lactate dehydrogenases (LDHs) have been highly focused for long time, due to their important roles in biochemical and metabolic pathways of cells. On the basis of genome-wide searching results, three putative LDH genes from Bacillus cereus ATCC 14579 genome have been PCR-amplified, cloned, and well-expressed in E. coli. All three BcLDH isozymes are supposed to share highly conserved catalytic amino acid residues in common $NAD^+$-dependent LDHs. Meanwhile, BcLDH1 consisting of 314 amino acids shares 86 and 49% of identities with BcLDH2 and 3, respectively. Interestingly, only BcLDH1 showed the converting activities between L-lactate and pyruvate in the presence of $NAD^+$ coenzyme, while the other isozymes are likely to have almost no activity. As a result, it was revealed that BcLDH1 can be a typical $NAD^+$-dependent L-lactate-specific dehydrogenase.

• Journal of Chest Surgery
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• v.15 no.4
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• pp.460-466
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• 1982

A analysis of CPK & LDH Isoenzyme was done on the consecutive patients undergoing thoracic operations from July 1982 to October 1982 in the Department of Thoracic and Cardiovascular Surgery, Capital Armed Forces General Hospital. Eighteen patients were analysed by three groups, such as open heart surgery [group A], major thoracic operation [group B] , minor thoracic operation group [group C]. In all patients serial determination of total level and Isoenzyme of CPK, LDH wad done on preoperative operative and up to 8th post-operative day, The results obtained are as follows. 1. The average value of serum CPK before the operation was 61 IU/L. The value of serum CPK was increased following the operation mainly MM portion and reached to the maximal level of 536107 IU/L in A group 1200191 IU/L in B group, 306150 IU/L in C group on the first postoperative day. The enzyme activity was gradually decreased thereafter and returned to the normal range on the 3rd or 4th day after the operation. 2. The average value of serum LDH before the operation was found to be 83 IU/L. The value was increased during the operation and reached to the maximal level of 481108 IU/L in group A, 14827 I U/L in group B, 10035 IU/L in group C on the second day after the operation. The enzyme activity was gradually decreased thereafter and returned to the normal range on the seventh day after the operation. The enzyme activity was dependent to the duration of operation, severity of muscle damage, type of thoracotomy, effect of extracorporeal circulation, state of disease.

• Journal of Life Science
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• v.14 no.4
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• pp.708-715
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• 2004

The lactate dehydrogenase (EC 1.1.1.27, LDH) in liver of Lempetra japonica was purified in buffer of affinity chromatography. The liver-specific $C_4$ isozyme of Gadus macrocephalus was purified by heat treatment, affinity chromatography, and DEAE-Sephacel chromatography. The liver-specific $C_4$ isozyme was eluted in a buffer containing NAD+ and was coeluted with $B_4$isozyme in plain buffer of affinity chromagraphy. Liver-specific $C_4$ isozyme in G. macrocephalus was the most thermostable, and$B_4$isozyme was more stable than $A_4$. The LDH in the fraction of pH 7.45 purified from the liver of L. iaponica by chromatofocusing was more inhibited by pyruvate than purified LDH. The optimum pH of the LDH isozyme in the liver of L. japonica was 7.5 and that of liver-specific$C_4$ isozyme was 8.5. The LDH in liver of L. japonica made complexes more with antibody against Coreoperca herzi$A_4$ and liver-specific $C_4$ than with that against eye-specific $C_4$. Therefore, the structure of the LDH in liver of L. japonica might be similarly evolved to that of subunit A and liver-specific $C_4$ isozyme in liver tissue of G. macrocephalus. The evolution rate of subunit C is faster than that of subunit A. LDH in liver of L. japonica has not one isozyme but isozymes and it was also found out to have not only subunit A and B but also subunit C.

• Journal of Life Science
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• v.26 no.2
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• pp.155-163
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• 2016

Metabolism of lactate dehydrogenase (EC 1.1.1.27, LDH) was studied to identify the function of LDH-C. Tissues of LDH liver-specific Ldh-C expressed Carassius auratus and eye-specific Ldh-C expressed Lepomis macrochirus after starvation were studied. LDH activity in liver tissue from C. auratus was increased after starvation. And LDH specific activity (units/mg) and LDH/CS were increased in tissues. It means the anaerobic metabolism was taking place in C. auratus after starvation. LDH B₄ isozyme was decreased in skeletal muscle and increased in heart tissue. LDH C₄ isozymes those showed in eye and brain tissues were identified as liver-specific C₄ isozymes and disappeared after starvation. And C hybrid in eye, A₄ isozyme in brain, and both C hybrid and C₄ isozyme in liver tissue were increased, respectively. In L. macrochirus, the level of variation of LDH activities was low but greatly increased especially in eye tissue and LDH A₄ and AC hybrid were increased in brain tissue. The LDH activities in tissues from C. auratus and L. macrochirus remained 30.30-18.64% and 25-18.75%, respectively, as a result of the inhibition by 10 mM of pyruvate. The Km^PYR values of LDH in C. auratus were increased. As a result, LDH liver-specific C₄ isozyme was expressed in liver, brain and eye tissues during starvation. It seems metabolism of lactate was predominant in brain tissue. After starvation, the liver-specific LDH-C was affected more than eye-specific LDH-C.

• Journal of Life Science
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• v.22 no.2
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• pp.209-219
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• 2012

The properties of lactate dehydrogenase (LDH, EC 1.1.1.27) eye-specific $C_4$ isozyme were studied by polyacrylamide gel electrophoresis, Western blotting, immunoprecipitation, and enzyme kinetics. Furthermore, we proposed the optimal conditions for measuring the activity of LDH eye-specific $C_4$ isozyme. The isozymes were detected in the cytosol of eye tissues from Lepomis macrochirus and Micropterus salmoides and were more similar to the $A_4$ than the $B_4$ isozyme. LDH/CS in the eye tissue of L. macrochirus was increased in September, so the ratio of anaerobic metabolism was high. The electrophoretic patterns of mitochondrial LDH were similar to those of cytosolic LDH in the eye tissues of L. macrochirus and Micropterus salmoides. LDH eye-specific $C_4$ isozyme from eye tissue was purified by preparative native-PAGE. The activities of LDH eye-specific $C_4$ isozymes in L. macrochirus and M. salmoides were reduced at concentrations greater than 0.2 mM and 0.1 mM of pyruvate, respectively. These concentrations remained at 5.2% and 15.8% as a result of the inhibition by 10 mM of pyruvate, so the degree of inhibition was very high. The LDH activities of eye tissues were reduced at concentrations greater than 22 mM and 24 mM of lactate, respectively, in L. macrochirus and M. salmoides. The ${K_m}^{PYR}$ of eye-specific $C_4$ was 0.088 mM in L. macrochirus and it was 0.033 mM in M. salmoides. The activities of cytosolic and mitochondrial eye-specific $C_4$ isozymes were high in ${\alpha}$-ketobutyric acid. Furthermore, the activities of eye tissue and eye-specific $C_4$ isozyme had to be measured with 0.5 mM of pyruvate and a buffer solution of pH 7.5. As a conclusion, the eye-specific $C_4$ isozyme in M. salmoides has a high affinity for pyruvate and exhibits maximum activity at a lower concentration of pyruvate and at higher concentration of lactate than that in L. macrochirus. Therefore, it seems that the energy produced by the LDH eye-specific $C_4$ isozyme in M. salmoides was used at the first stage of predatory behavior.