• Title/Summary/Keyword: LDH isozyme

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Metabolic Adjustment of Lactate Dehydrogenase Isozymes to a Change in Dissolved Oxygen in Bluegill (Lepomis macrochirus) (파랑볼우럭(Lepomis macrochirus)에서 용존산소량의 변화에 대한 젖산탈수소효소 동위효소들의 대사조절)

  • Ku, Bora;Cho, Sung Kyu;Yum, Jung Joo
    • Journal of Life Science
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    • v.31 no.12
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    • pp.1066-1071
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    • 2021
  • The aim of this study was to examine the metabolic adjustment of lactate dehydrogenase (EC 1.1.1.27, LDH) isozymes to a change in dissolved oxygen (DO) in bluegill (Lepomis macrochirus). After bluegills were adapted to a constant environment in an aquarium, the DO was changed to investigate the activity of LDH isozyme and the relative ratio of subunits A, B, and C for each tissue. When the DO was decreased from 18 ppm to 6 ppm, LDH in skeletal muscle, heart, and brain tissues recovered to the level of control activity within 12, 12, and 6 hr, respectively. LDH activity changed in accordance with a change in DO. The compensation was performed rapidly and is thought to be an important function of LDH in enabling bluegills to adapt to their environment. In bluegill heart, eye, and brain tissues, the relative ratio of subunit A increased and showed a tendency to recover similarly to the subunit ratio of control groups up to 12 hr. It is thought that the anaerobic metabolism using subunit A was increased in the initial stage when DO was changed. In addition, the results revealed that subunit C was more similar to subunit A than subunit B. In bluegills, subunits A and C of LDH seem to be evolutionarily similar. LDH isozymes, mainly containing subunits A and C, are likely responsible for the function of pyruvate reductase, which plays a role in making the bluegill adapt to a hypoxic environment through anaerobic metabolism.

Metabolic Adjustments of Lactate Dehydrogenase Isozymes to the Environmental Temperature in Bluegill (Lepomis macrochirus) (환경온도에 대한 파랑볼우럭(Lepomis macrochirus) 젖산탈수소효소 동위효소들의 대사조절)

  • Ku, Bora;Cho, Sung Kyu;Yum, Jung Joo
    • 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 KmPYR 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.

Effect of Mitochondrial Inhibitor on Lactate Dehydrogenase of Mesocricetus auratus and Bos taurus coreanae (햄스터와 소의 젖산탈수소효소에 대한 미토콘드리아 inhibitor의 영향)

  • Cho Sung Kyu;Lee Sang Hak;Yum Jung Joo
    • Journal of Life Science
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    • v.15 no.1 s.68
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    • pp.100-105
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    • 2005
  • The lactate dehydrogenase (EC 1.1.1.27, LDH) inhibitors were isolated from the LDH-free crude mitochondrial fraction of skeletal muscle in Syrian hamster (Mesocricetus auratus) and Korean native cattle (Bos taurus coreanae). The LDH inhibitor in skeletal muscle of M. auratus was successfully isolated by the treatment with 175 mM NaCl and ultrasonic. The LDH inhibitor in skeletal muscle of B. taurus coreanae was highly stable to heat and LDH fu isozyme was largely inhibited by the LDH inhibitor. The molecular weight of inhibitor was 22 kDa. Inhibitor played an important role in the binding of LDH with the mitochondria in tissues of skeletal muscle, kidney and liver except heart.

Transcriptional Control of Lactate Dehydrogenase A-Gene Expression during the Pre-replicative Phase of Regenerating Rat Liver (백서 재생간조직의 낙산탈수소효소 A-유전자 발현의 전사활성)

  • Kim, Hae-Young;Lee, Seung-Ki
    • 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.

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Nutritional and Biochemical Studies on the Pollen Load. -3. The Effect of Pollen Load on the Chloroform-induced Hepatic and Renal Damage in Rats- (화분립(花粉粒)의 영양생화학적(營養生化學的) 연구(硏究) -3. Chloroform에 의한 Rat의 간(肝) 및 위장(胃臟) 장해(障害)에 미치는 영향(影響)-)

  • Kwon, Chong-Suk;Yoon, Soo-Hong
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.15 no.3
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    • pp.235-242
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    • 1986
  • The present experiment was intended to determine the effect of pollen load on chloroform-induced hepatic and renal damage in rats. The subjects were administered with the graded concentration of chloroform and an additional amount of pollen to some groups, and the result of which was: 1. The content of total lipid in liver and kidney increased in proportion to the chloroform concentration, but decreased in the chloroform and pollen administration groups. 2. The amount of total cholesterol in serum, liver and kidney of the chloroform administration group was higher than that of the control group, and it decreased gradually with pollen administration. 3. The activity of sGOT, sGPT, and LDH increased in proportion to the chloroform concentration, but decreased in the pollen-treated groups. 4. It is not significant that the cellulose acetate electrophoresis of LDH isozymes showed the increased of $LDH_5$ in liver of the pollen administration group. LDH isozymes in kidney are not significantly changed, too.

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Studies on the Physiological Chemistry of the Spring Growth Habits in Naked Barley V. Changes in the Isozyme Patterns and Activities of Peroxidase During the Differentiation (과맥의 파성에 대한 생리화학적 연구 V. 유수의 분화, 발육과정중 Peroxidase의 활성 및 Isozyme Pattern)

  • 최선영;이강수;박기훈
    • KOREAN JOURNAL OF CROP SCIENCE
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    • v.31 no.3
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    • pp.375-382
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    • 1986
  • This study was carried out to obtain the basic information for the clarification of spring growth habits mechanism of naked barleys. The isozyme patterns and activities of peroxidase in the young spike and leaf blade were analyzed during the differentiation and development of young spike. The characteristic differences between the normal and rosetted type were in c and g isozymes in young spike, and in i isozyme in the leaf blade. In the normal type, c and i isozymes disappeared at the stage of spi-kelet differentiation, g isozyme at the stage of flolet differentiation. But, in the rosetted type, those three isozymes remained in dark stained condition until the time of final sampling. Especially, those three isozymes were higher in the rosetted type than those in the normal type even at the stage of bract differentiation(BDS), just prior to the reproductive stage. The activities of peroxidase decreased slowly after BDS in the young spike and leaf blade in the normal type, While, in the rosetted type, increased linearly, and the degree of increasing was remarkable in the young spike. It was interesting that the degree of activities in young spike was higher in the rosetted type than that in the normal type even at BDS. From the above results, the remarkable differences of the isozyme patterns and activities at BDS between the normal and rosetted type were considered to be the physiological expression of the varieties concerned with the degree of spring growth habits.

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A Biochemical Study for the Development of Genetic Marker on Salmonids in Korea (한국산 연어류에서 Genetic Marker 개발을 위한 생화학적 연구)

  • HONG Kyung-Pyo;MYOUNG Jung-Goo;SON Jin-Ki;PARK Chul-Won
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.27 no.1
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    • pp.83-88
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    • 1994
  • For the purpose of genetic stock indentification of three species of salmonid fishs and their hybrid, lactate dehydrogenase(LDH), malate dehydrogenase(MDH), isocitrate dehydrogenase(IDH), a-gylycerophosphate dehydrogenase(a-GPDH), malic enzyme(ME), 6-phospho-gluconate dehydrogenase(6-PGD), phosphoglucose isomerase(PGI) and phospho-glucomutase(PGM) from skeletal muscle, liver, heart and gill tissues in all three species were analyzed. Chum and masu salmon showed no polymorphic patterns in all isozyme loci, however rainbow trout were found to have polymorphic patterns at MDH-B, LDH and IDH loci. Especially, significant differences were found at MDH-B loci between the three species and the IDH patterns of rainbow trout were also different from the other two species. These loci therefore can be utilized as efficient genetic markers for the identification of hybrids and improve the efficiency of fish breeding. There was no difference except PGI between diploid and triploid isozyme patterns but PGI showed some potential as a marker for triploid in masu salmon.

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The Effect of Autoxidized Methyl Linoleate on the Serum Enzyme Activity in the Mouse (Acute Toxicity) (자동산화 Methyl Linoleate가 Mouse혈청의 효소활성에 미치는 영향 (급성 독성))

  • Paik, Tai-Hong;Chung, Nak-Seung
    • Journal of the Korean Applied Science and Technology
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    • v.1 no.1
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    • pp.23-31
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    • 1984
  • In order to investigate the acute toxicity of autoxidized methyl linoleate(AOML) on the activity of serum enzymes in the mouse, we administered once 0.45ml of AOML to ICR strain mouse by using stomach tube. The following results were obtained: The total lactic dehydrogenase(LDH) activities in the serum of AOML group were generally increased than those of normal group. According to electrophoresis, the activities of LDH, were increased while those of LDH, were decreased. The activities of glutamic oxaloacetic transaminase(GOT), glutamic-pyruvic transaminase(GPT) and ${\alpha}-amylase$ in the serum of AOML group were increased more than those of normal group. The activities of alkaline phosphatase in the serum of AOML group were increased but those of isozyme were not confirmed in the normal and AOML group. In the serum protein of AOML group, albumin was increased, on the other hand ${\gamma}-globulin$ was decreased. At the peripheral blood slide smear, lymphocytes were significantly decreased but neutrophils were increased and the morphological change of erythrocytes was observed. From these results we conclude that the AOML fed to mouse influences on the activity of various serum enzymes and blood cells in the mouse.