• The Korean Journal of Zoology
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• v.16 no.1
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• pp.55-65
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• 1973

MDH and LDH isozymes of various tissues of serveral snakes which belong to Colubridae, Crotalidae and Viperidae were studied. MDH isozymes were appeared as two bands in all species. Four LDH isozymes were found inall species of Colubridae, Crotalidae and Viperidae. LDH isozymes of muscle and liver had fundamentally the same pattern. On the other hand, there were two LDH isozymes in the heart of all species and the pattern of heart LDH isozyme was reverse of the pattern in muscle. The pattern of LDH isozymes of stomach tissue can be thought as the same pattern with that of heart in all species, but in the stomach tissue of Crotalidae and Viperidae there were four LDH isozymes.

• 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.

• 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.

• 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.

• 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.

• 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.

• Journal of Preventive Medicine and Public Health
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• v.16 no.1
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• pp.79-88
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• 1983

There has been some evidence concerning the fact that trihalomethanes(THMs), toxic chlorinated compounds, may be present in drinking water. One of the important methodologies to evaluate the toxicity of THMs is to determine enzyme alteration in experimental animal tissues after treatment. This study was intended to investigate how lactic dehydrogenase(LDH) of rat tissues is affected by administration of chloroform($CHCl_3$) and dichloromonobromomethane($CHCl_2\;Br$). THMs, high dose(1/10 LD50) or low dose(1/50 LD50) of $CHCl_3$ or $CHCl_{2}Br$ were administered orally to experimental rats for 4 or 8 weeks. The treated groups of rats were sacrificed to determine LDH specific activity and isozyme pattern in various organs which were liver, thigh muscle, kidney and brain. The conclusions were obtained as follows: 1. Alteration of LDH activities and isozyme patterns were revealed before morphologic changes in tissues. 2. The LDH specific activities were increased significantly in liver and brain after administration of high concentrations of $CHCl_3$ and $CHCl_{2}Br$ for 4 weeks respectively. Otherwise, they were decreased significantly in liver, muscle and kidney after administration for 8 weeks. 3. The isozyme activities of LDH-4 and LDH-5 were increased in muscle, brain, and especially the liver. 4. It was more distinct for the decrement of LDH H-type isozyme than the increment of M-type isozyme in muscle.

• 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.

• 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.

• 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.