• The Korean Journal of Zoology
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• v.36 no.3
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• pp.319-328
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• 1993

All vertebrates other than lampreys exhibit multiple loci encoding lactate dehydrogenase (EC 1.1.1.27,LDH). From the result shown by cellulose acetate and starch gel electrophoresis, the lampreys were-reported to have only one isozyme. However in our results the LDH of skeletal muscle, heart and kidney in Lampetra japonica were separated into three isozymes and that of liver was separated into two isozymes by polyacrylamide gel electrophoresis. The LDH of skeletal muscle and heart were separated into four isozymes and that of liver was separated into two isozymes by polyacrylamide gel isoelectric focusing (PAGlEF). The LDH of skeletal muscle were separated into four isozymes through the chromatofocusing. The molecular weight of LDH isozymes in skeletal muscle was approximately estimated to be 140,000 by Sephadex G-200 gel filtration. The LDH isozymes of skeletal muscle, heart and liver were inhibited by pyruvate to the nearly similar degree. And the degree of inhibition by pyruvate showed the value between LDH A$_4$and LDH B$_4$isozyme. And the LDH isozymes in heart, liver and skeletal muscle were thermostable. The results mentioned above indicate that the LDH isozyme in lamprey (Lampetra japonica) has not one isozyme but isozymes. And it is also found out that the two structures of their subunits are similar each others.

• The Korean Journal of Zoology
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• v.35 no.1
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• pp.102-106
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• 1992

진도개와 삽사리 혈청 lactate dehydrogenase와 혈청 alkaline phosphatase의 동위효소 및 효소활성도를 분석하였다. 전기영동결과 진도개와 삽사리의 혈청에서는 5두지 종류의 LDH의 동위효소가 모두 확인되었다. LDH의 활성도는 진도개의 경우 522.53 $\pm$ 279.96(U/L)이었고 삽사리는 534.10 $\pm$ 280.35(U/L)이었다. 진도개와 삽사리의 혈청 alkaline phosphatase전기 영동상에서 는 한 종류의 동위효소만 관찰되었고 활성도는 진도개의 경우 7.61 $\pm$ 4.52(K-A unit)였고 삽사리는 10.46 $\pm$ 7. 10(K-A unit) 였다. 삽사리의 ALP 활성도는 연령에 따라 커다란 차이를 나타내었다.

• Journal of Life Science
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• v.18 no.2
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• pp.264-272
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• 2008

The lactate dehydrogenase (EC 1.1.1.27, LDH) isozymes in tissues from Acanthogobius hasta were characterized by biochemical, immunochemical and kinetic methods. The activities of LDH in skeletal muscle and eye tissues were 65.30 and 53.25 units, but LDH activities in heart and liver tissues were very low. LDH/CS (EC 4.1.3.7, citrate synthase) in skeletal muscle was the highest as 22.29. Specific activities of LDH in brain, eye and skeletal muscle were 56.45, 38.04 and 11.0 units/mg, respectively. The LDH isozymes in tissues were separated by polyacrylamide gel electrophoresis after immunoprecipitation with antiserum against $A_4,\;B_4$ eye-specific $C_4$ and liver-specific $C_4$. LDH $AC_4$ isozymes were detected predominantly in skeletal muscle, brain and eye tissues, and $B_4$ isozyme was detected in heart. Anodal eye-specific $C_4$ and cathodal liver-specific $C_4$ were coexpressed in A. hasta. The eye-specific $C_4$ isozyme showed higher activity in eye tissue, but liver-specific $C_4$ isozyme showed lower activity in liver. As a result, one part of molecular structures in $A_4\;and\;C_4,\;A_4\;and\;B_4$, and eye-specific $C_4$ and liver-specific $C_4$ were similar, but in $B_4\;and\;C_4$ were different with each other. Therefore the subunit A may be conservative in evolution, and the evolution of subunit B seems to be faster than that of subunit A. The LDH $A_4$ isozyme of skeletal muscle was purified in the fraction from elution with NAD+ containing buffer of affinity chromatography and eye-specific $C_4$ isozyme was eluted right after $A_4$, so the structure of eye-specific $C_4$ isozyme is similar to $A_4$. And LDH activity remained 35.22-43.47% as a result of the inhibition by pyruvate, the Michaelis-Menten constant values for pyruvate was 0.080-0.098 mM, and Vmax were 153.85 units, 35.09 units in skeletal muscle and eye, respectively. Also the $B_4$ isozyme was the thermo-stablest and $C_4$ was stabler than $A_4$ isozyme. The optimum pH of LDH was 6.5. The results mentioned above indicate that isozymes in tissues showed the properties between LDH $A_4\;and\;B_4$ isozyme as A. hasta was adapted to hypoxic conditions. Also LDH seems to function more effectively under anaerobic condition because LDH in skeletal muscle and eye tissues have high affinity for pyruvate.

• Journal of Life Science
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• v.26 no.10
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• pp.1105-1112
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• 2016

The aim of this study was to examine the metabolic adjustment of lactate dehydrogenase (EC 1.1.1.27, LDH) isozymes to the environmental temperature in bluegill (Lepomis macrochirus). This study included three groups of bluegill collected in April (group Ⅰ), May (group Ⅱ), and September (group Ⅲ). The LDH activities of skeletal muscle, heart, and brain tissues were higher in group Ⅲ than in groups Ⅰ and Ⅱ. The citrate synthase (EC 4.1.3.7, CS) activity was higher in skeletal muscle but lower in heart and brain tissues of group Ⅱ as compared to group Ⅰ. In contrast, the CS activity was lower in skeletal muscle and higher in heart and brain tissues in group Ⅲ than in group Ⅱ. Furthermore, the LDH/CS activity ratio was higher in the skeletal muscle and brain in group Ⅲ than in groups Ⅰ and Ⅱ. Accordingly, anaerobic metabolism was increased in group Ⅲ. LDH A₄, A₂B₂, and B₄ isozymes were expressed in skeletal muscle, heart, liver, and brain tissues. The LDH C hybrid was detected in brain tissue. The LDH A₄ isozyme was successfully purified by affinity chromatography. The molecular weight of the purified LDH A₄ isozyme was 136 kDa and its optimal pH for enzymatic activity was 8.0. The K_m^PYR values of LDH in skeletal muscle were 0.161-0.227 mM using pyruvate as a substrate. These kinetic properties of LDH in skeletal muscle are consistent with the fact that bluegill is a cold-adapted species. These results may be useful for predicting the habitat use of this fish.

• 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.

• Proceedings of the Zoological Society Korea Conference
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• 2000.10a
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• pp.207.1-207
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• 2000

No Abstract, See Full Text

• Journal of Nutrition and Health
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• v.49 no.2
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• pp.63-71
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• 2016

Purpose: Skin pH, an indicator of skin health, is maintained by various organic factors, which include lactate, free amino acid (FAA), and free fatty acid (FFA). As skin ages or with illness, skin pH becomes less acidic, and functional food has been developed to maintain the acidic pH of skin. In this study, we determined the dietary effect of green tea extract (GTE) on skin pH of photo-aged mice, as measured by epidermal levels of lactate, FAA, and FFA. The protein expression and activity of lactate dehydrogenase (LDH), an enzyme of pyruvate reduction for lactate generation, was further determined. Methods: Albino hairless mice were fed a control diet (group UV+) or a diet with 1% GTE (group GTE) in parallel with UV irradiation for 10 weeks. A normal control group was fed a control diet without UV irradiation for 10 weeks (group UV-). Results: Skin pH was higher (less acidic) in group UV+ than in group UV-. In parallel, epidermal levels of lactate and FFA, as well as of LDH protein expression and activity, were reduced in group UV+. Dietary supplementation of GTE (group GTE) reduced skin pH to similar to the level of group UV-, and inversely increased epidermal levels of lactate, LDH protein expression and activity, but not of FFA. Although epidermal levels of FAA were similar in groups UV- and UV+, it was increased in group GTE to a level higher than in group UV-. In further analysis of major FFA, epidermal levels of palmitic acid [16:0], oleic acid [18:1(n-9)], and linoleic acid [18:2(n-6), but not of stearic acid [18:0] in group GTE were similar to or lower than those in group UV+. Conclusion: Dietary GTE normalized skin pH with increased levels of lactate and FAA, as well as with increased protein expression and activity of LDH in the epidermis of UVB irradiated hairless mice.

• The Korean Journal of Zoology
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• v.27 no.2
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• pp.85-92
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• 1984

The effect of copper ion on the lactate dehydrogenase isozyme patterns in the heart, liver, kidney, skeletal muscle, and ovary of catfish, Parasilurus asotus, was studied by cellulose acetate gel electrophoresis. 1. The LDH-1 and LDH-2 of heart type appeared in the heart muscle of control fish. When the fish were exposed to copper ion, however, the LDH-1, LDH-2, LDH-3, and LDH-4 appeared. The amount of LDH-1 was decreased and those of LDH-2, LDH-3, and LDH-4 were increased. 2. There was one band of LDH-4 in the liver of normal fish. But the amount of LDH-4 was decreased and additional new LDH-5 appeared by exposure to copper ion. 3. There were LDH-1, LDH-2, and LDH-4 in the kidney tissue of both control and experimental groups. The LDH-1 was increased, whereas LDH-2 and LDH-4 were decreased after exposure to copper ion. 4. There was broad band of LDH-5 in the skeletal muscle of the control fish. However, the LDH-4 and LDH-5 with M sub-band appeared by the exposure to copper ion. 5. There was LDH-3 band only in the ovary of control, wheras all five LDH isozymes appeared in the ovary of the fish exposed to copper iion. 6. During the period of exposure to copper ion, the LDH isozyme of heart type which associated with aerobic metabolism was decreased, but the LDH isozyme of muscle type of anaerobic metabolism was increased in most of heart, liver, and skeletal muscle. It seems that these organs are related to some of important functions for anaerobic metabolism during the copper poisoning period.

• International Journal of Industrial Entomology and Biomaterials
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• v.15 no.2
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• pp.137-143
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• 2007

Lactate dehydrogenase (LDH) is a ubiquitous enzyme that plays a significant role in the clinical diagnosis of pathologic processes. Discovery of the LDH (BmLDH) gene in B. mori may shed light on its role in the biology of Lepidoptera species, and afford further understanding of the function of the enzyme. In this study, we used the bioinformatics tools to identify LDH gene in B. mori. Sequence analysis showed that BmLDH cDNA contains a 996 bp open reading frame, encoding 331 AA proteins, with seven introns. Compared with hHLDH (human heart LDH), BmLDH contained the same key active sites. Domain search and protein fold recognition analyses provide compelling evidences that the deduced protein is a LDH. Using the computer program MEGA3, we conducted a search for homologs of BmLDH among many eukaryotic species and confirmed that the BmLDH was conserved in all organisms investigated. This gene has been registered in GenBank under the accession number EU000385.

• YAKHAK HOEJI
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• v.20 no.1
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• pp.92-96
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• 1976

A series of experimental groups has been studied in the state of hypolycemia caused by a single intraperitoneal injection of insulin after 24 hrs of fasting albino rats and then the variation of LDH activities and LDH isozyme patterns in the liver, muscle and serum had been reported. The total LDH activity has been elevated in the liver and the muscle above the average level for control group, but increased continusly during 20 min and decreased in the 20-45 min intervals and increased again 45 min in the serum. The change of LDH isozyme patterns had been shown that in the liver LDH$_{5}$ was increased, LDH$_{4}$ was decreased and in the muscle LDH$_{1}$ was diminished by 30 min ws restored again after 45 min and LDH$_{2}$ decreased about 94 percentage at 30 min, decreased by 45 min and increased greater again after 45 min and in the muscle LDH$_{3}$, LDH$_{4}$, and LDH$_{5}$ were increased to the greatest by 20 min, decreased in 20-45 min intervals and increased again after 45 min.