• The Korean Journal of Zoology
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• v.15 no.3
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• pp.101-104
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• 1972

A simple and economical method for separation of lactate and malate dehydrogenase isozymes is described in detail. The method is based on cellulose acetate strip electrophoretic separation of the isozymes, tetrazolium reduction to purple formazan. Resolution is as good as in the experiment using expensive equipments.

• The Korean Journal of Zoology
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• v.23 no.4
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• pp.263-272
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• 1980

Polyacrylamide gel electrophoresis was used to investigate the patterns of LDH and MDH isozymes in the embryo and adult of amphibia; Rana nigromaculata, Rana plancyi chosenica and Hynobius leechii. Rana nigromaculata is considered to be heterozygous for the gene specifying the "B" subunit of LDH, and Hynobius leechii to be heterozygous for the gene specifying the "A" subunit of LDH. The LDH isozyme paatern of embryos of the above three species is characterized by a gradual increase in the activity of LDH-5 (muscular form)during development. Two or three molecular forms of MDH is present steadily from early embryos and in adult. Of the MDH isozymes, the more cathodic one (MDH-m) appears weakly in early developing stages, but increases slowly in the activity as the embryo develops.the embryo develops.

• Journal of Life Science
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• v.24 no.2
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• pp.118-127
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• 2014

The kinetic properties and isozyme expression of lactate dehydrogenase (EC 1.1.1.27; LDH) in tissues from Rana catesbeiana I and II collected from February (I) and August (II) were studied. LDH activities, A4 isozyme, and LDH/citrate synthase (EC 4.1.3.7; CS) were high in skeletal muscle from R. catesbeiana I, and LDH $B_4$ isozyme increased in several tissues of R. catesbeiana II. In particular, LDH activities were high in heart and brain tissues from R. catesbeiana II. LDH eye-specific C isozyme, detected by native polyacrylamide gel electrophoresis after immunoprecipitation, was expressed in eye tissue and was more similar to the $B_4$ than $A_4$ isozyme. LDH $A_4$ isozyme was purified by oxamate-linked affinity chromatography, and the molecular weight of subunit A was 32.0 kDa. In R. catesbeiana II, levels of $Km^{PYU}$, $Vmax^{LAC}$, and tolerance to lactate of LDH were high in all tissues, and $Vmax^{PYU}$ of LDH in heart and brain tissue was highly detected. Purified $A_4$ isozyme and LDH in eye tissue were highly tolerate compared to others. The $Km^{LAC}$ value was highly measured compared to $Km^{PYU}$. The degree of inhibition by 10 mM of pyruvate on LDH activities in tissues from R. catesbeiana I and II was more pronounced as the ratio of subunit B increased. As a result, characteristic expression of LDH eye-specific C was found in R. catesbeiana. Anaerobic metabolism seemed to predominate as the LDH of skeletal muscle from I showed higher activity. It also appeared that R. catesbeiana II adapted well to incremental increases in LDH B, becoming tolerant to the lactate of LDH in tissues.

• The Korean Journal of Zoology
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• v.15 no.3
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• pp.105-110
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• 1972

A cellulosse acetate electrophoretic survey of Korean Anura has revealed the presence of diverse lactate and malate dehydrogenase (LDH and MDH) isozymes. The pattern of LDH and MDH isozymes in the tissues of the central nervous system of the six species of Anura examined are species specific and differ from those of mammals and birds. Both Rana nigromaculata nigromaculata and Rana nigromaculata coreana have two molecular forms of LDH and MDH, respectively, with almost the same pattern. Whole brain homogenate of Rana temporaria shows also a maximum of only two LDH isozymes. Both Bufo bufo asiaticus and Bombina orientalis have five molecular forms of LDH with an entirely different spacing on the zymograms, whereas Rana rugosa has three. Two molecular forms of MDH are present in all animals examined and one band is shown in olfactory lobe and mixture of cerebellum and medulla oblongata of Rana nigromaculata nigromaculata.

• 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

• 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.

• 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.27 no.5
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• pp.530-535
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• 2017

Mitochondria were isolated from bird and mammals. The activity of monoamine oxidase (EC 1.4.3.4) was then measured to identify mitochondrial isolation. Lactate dehydrogenase (EC 1.1.1.27, lactate dehydrogenase, LDH) isozymes in mitochondrial fractions were analyzed by biochemical and immunochemical methods. The activity of mitochondrial LDH was lower in mammals than in bird. Therefore, the role of mitochondrial LDH seems to be more important in bird than in mammals. The concentration of protein in all tissues of bird and mammals was less in the mitochondria than in the cytosol. In the cytosol of mice and golden hamsters, testis-specific LDH $C_4$ isozyme was expressed in testis in addition to the LDH $A_4$, $A_3B$, $A_2B_2$, $AB_3$, and $B_4$ isozymes. A single LDH AB hybrid isozyme was expressed in the chicken mitochondria. In mammals, mitochondrial LDH isozymes were differed according to tissues. LDH $A_4$ and testis-specific LDH $C_4$ isozymes were expressed in the mitochondria of mice. The mitochondrial testis-specific LDH $C_4$ isozyme was expressed only in the mice. In the golden hamster mitochondria, the LDH $B_4$ isozyme functioned as a lactate oxidase. As our results show, the mitochondrial LDH seemed to be playing the different role in the bird and mammals in relation with their metabolic conditions and habitats.

• Korean Journal of Animal Reproduction
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• v.17 no.3
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• pp.257-262
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• 1993

Various tissue and follicular components were analyzed for the determination of lactate dehydrogenase(LDH) isozyme patterns by electrophoretic technique with chromogen reaction in the pig. Optimum conditions for the tissue homogenate and the storage were finally established. Small quantities of follicular components were analysed for typing of LDH isozymes by microelectrophoresis. Microelectrophoretic analysis showed that only LDH-1 was visible in the oocytes, all isozymes in cumulus masses, and LDH-1, 2 and 3 in follicular fluid. The results provide critical information on the LDH activity of various tissues and follicular components. Furthermore, t he developed methods should be useful the analysis of LDH in the small quantity of samples, especially in the oocyte, and easily applicable to the oocyte and early embryos of other domestic species.

• Journal of Life Science
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• v.21 no.11
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• pp.1565-1572
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• 2011

Eye-specific lactate dehydrogenase (EC 1.1.1.27, LDH) $C_4$ isozyme in the eyes of greenlings (Hexagrammos otakii) was successfully purified by affinity chromatography and continuous-elution electrophoresis. The molecular weight of the purified eye-specific LDH $C_4$ isozyme was 154.8 kDa, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Optimal pH for enzymatic reaction of the eye-specific LDH $C_4$ isozyme was pH 8.5. $K^{PYR}_m$ value of the purified eye-specific LDH $C_4$ isozyme was $1.88{\times}10^{-5}$ M using pyruvate as a substrate. These results indicate that we must consider pH when measuring eye-specific LDH $C_4$ isozyme activity. The eye-specific LDH $C_4$ isozyme had a higher binding affinity for the substrate as a pyruvate than LDH A4 isozyme. Antibodies produced against the purified eye-specific LDH $C_4$ isozyme may be used in the diagnosis of several human diseases and in comparative physiological studies of fishes.