• Title/Summary/Keyword: 동위효소

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Changes of LDH Subunit Combinations Induced by Tetrodotoxin (Tetrodotoxin에 의하여 유발되는 LDH 하부단위체 조합의 변화)

  • Kim, Sang-Yeop;Yum, Jung-Joo
    • The Korean Journal of Zoology
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    • v.28 no.4
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    • pp.227-236
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    • 1985
  • In an attempt to make a scrutiny into a mechanism for the formation of quaternary structure of LDH isozymes, male mice were intraperitoneally exposed to a wide range of tetrodotoxin concentration and the changes in relative percentage of the five isozymes were monitored by electrophoresis and subsequent densitometry. The observations that a conspicuous increase of the $H_4$ isozyme was demonstrated in nearly all brain tissues, that the $M_4$ isozyme of skeletal muscle tissue was slightly increased while the $M_3H$ and $M_2H_2$ isozymes were decreased, that the M/H ratio was strikingly reduced in heart tissue and that assembly of $H_4$ isozyme was revealed in liver tissue although its rate was extremely low suggest that new intracellular ionic environment established by compulsory change in Donnan equilibrium could alter the LDH isozyme distribution. The reduction of assembly of $M_3H$ isozyme found in mouse tissues exposed to tetrodotoxin also seems to suggest that the subunit combination of 3M+H is very unfavorable in an intracellular environment deviated from its accustomed one. It was reaffirmed that there might occur TTX-insensitive sodium channels in plasma membrane.

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Distribution and Role of Mitochondrial Lactate Dehydrogenase Isozymes in Bird and Mammals (조류 및 포유류 내 미토콘드리아 젖산탈수소효소 동위효소들의 분포와 역할)

  • Cho, Sung Kyu;Yum, Jung Joo
    • 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.

Isozymic Characteristics of Multiple-Ear and Tiller Maize Lines (다수다얼성 옥수수의 동위효소 특성)

  • ;Bong-Ho Chae
    • KOREAN JOURNAL OF CROP SCIENCE
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    • v.32 no.1
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    • pp.16-23
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    • 1987
  • This experiment was conducted to determine the isozymic differences between normal maize and maize inbreds of multiple ears and tillers (MET). Two maize inbreds Euisung, Iri and their hybrid having tillers and multiple ears were compared with normal maize. With usual electrophoresis using 6% polyacrylamide gel, peroxidase and esterase enzymes were studied. Matured leaf, culm, leaf sheath, root and young ear tissues showed different isozymic patterns between METs and normal maize in peroxidase. The Euisung inbred grown for 7 days under dark condition showed typical peroxidase. bands compared with checks in the tissues of coleoptile and stele. Better observation of isozymic bands was made during early part of maize growth. Parental inbreds showed more active and apparent band differences than their hybrids in esterase. Bands for esterase were also apparently different in the stele, coleoptile and young ear tissues of the METs and the checks. The maize lines infected with black streaked dwarf virus showed obvious differences in peroxidase and esterase isozymes.

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Inheritance and Linkage of Some Polymorphic Isozymes in Ginkgo biloba L. (은행나무의 몇가지 다형적(多形的) 동위효소(同位酵素)의 유전양식(遺傳樣式) 및 연관(連關))

  • Kwon, Hae-Yeun;Kim, Zin-Suh
    • Journal of Korean Society of Forest Science
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    • v.89 no.4
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    • pp.527-535
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    • 2000
  • Isozyme variants of 15 enzyme systems were analyzed in megagametophytes of Ginkgo biloba L. Five enzyme systems (ADH, G6PD, IDH, MPI, and UGPP) appeared to be monomorphic. Only 11 isozyme zones observed in 10 enzyme systems were polymorphic : ACON-A, FST-B, GDH-A, GOT-B, MDH-B, MDH-C, MNR-A, PGI-B, PGM-A, 6PGD-B and SKDH-B. The segregation ratio and heterogeneity at most polymorphic zones suggested that each isozyme zone was controlled by a single locus with codominant alleles, but significant deviation from 1 : 1 segregation was observed at MDH-B in pooled data. Three pairs of isozyme loci (ACON-A : MDH-B, GOT-B : PGI-B, and MNR-A : SKDH-B) were found to be weakly linked. Recombination frequencies between them ranged from 0.38 to 0.40 (p<0.05).

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Changes of Activities and Isozymes of Lactate Dehydrogenase in Coreoperca herzi and Pseudogobio esocinus Acclimated to Rapid Increase of Dissolved Oxygen (급격한 용존산소량 증가에 순응한 꺽지(Coreoperca herzi)와 모래무지(Pseudogobioesocinus) 젖산탈수소효소 활성과 동위효소의 변화)

  • Cho Sung Kyu;Yum Jung Joo
    • Journal of Life Science
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    • v.15 no.1 s.68
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    • pp.71-79
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    • 2005
  • The metabolism of lactate dehydrogenase (EC 1.1.1.27, LDH) and $C_4$ isozyme were studied in tissues of Coreoperca herzi and Pseudogobio esocinus acclimated to rapid increase of dissolved oxygen (DO). In C. herzi the LDH activity was changed $35-39\%$ in brain and liver tissues, and within $20\%$ in other tissues. The $B_4$ isozyme was increased and isozyme containing subunit C was decreased in muscle tissue. The $B_4$ isozyme was increased in heart and kidney. In P. esocinus, the LDH activity in liver tissues was largely increased to $150\%$ for 30 minute and $70\%$ in other tissues. The $A_4$ isozyme was increased in muscle and $B_4$ isozyme was increased in other tissues. Especially, the metabolism of liver tissue in P. esocinus was regulated by increasing liver-specific $C_4$ and decreasing $A_4$ isozyme. But the metabolism of eye tissue in C. herzi was regulated by decreasing LDH activity and eye-specific $C_4$ isozyme. The LDH activity and LDH isozyme in P. esocinus were largely increased than C. herzi acclimated to rapid increase of DO. And eye-specific $C_4$ and liver-specific $C_4$ isozymes played role as lactate oxidase. Therefore, the response of species acclimated to rapid increase of DO seems to be variable, perhaps due to prior exposure to environmental conditions.

Characterization and Evolutionary Relationship of Lactate Dehydrogenase in Liver of Lampetra japonica and Liver-specific C4 Isozyme in Gadus macrocephdus. (칠성장어(Lampetra japnica) 간조직 젖산탈수소효소와 대구(Gadus macrocephalus) liver-Specific C4동위효소의 특성 및 진화적 관계)

  • 박선영;조성규;염정주
    • 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.

Biochemical Properties of Lactate Dehydrogenase Eye-Specific C4 Isozyme: Lepomis macrochirus and Micropterus salmoides (젖산탈수소효소 eye-specific C4 동위효소의 생화학적 특성: 파랑볼우럭(Lepomis macrochirus)과 큰입우럭(Micropterus salmoides))

  • Yum, Jung-Joo;Ku, Bo-Ra
    • 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.

신호 전달 체계에 있어서의 Phospholipase C에 대한 연구

  • 민도식;김재호;이영한;서판길;류성호
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 1992.05a
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    • pp.27-27
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    • 1992
  • 많은 홀몬, 성장인자 및 신경 전달물질들은 각각에 대한 세포막의 수용체와 결합하여 Phospholipase C (PLC)를 활성화시키므로서 신호를 세포내로 전달하여 세포의 성장, 대사, 신경 흥분, 수축 및 분비 등의 생리 현상을 나타내고 있다. 이 신호 전달의 중심 효소인 PLC는 현재까지의 효소 분리, 유전자 클로닝 등의 방법으로 3가지 Class에 적어도 8종유의 등위효소(Isozyme)들이 존재하고 있는 것으로 밝혀지고 있다. 본 연구에서는 이와 같은 등위효소에 특이적인 조절 물질을 선별할 수 있는 체계를 확립하기 위하여 새로운 동위효소의 분리 및 규명과 이 동위효소들에 대한 과발현 및 발현 세포주 개발을 추진하고 있다.

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한국 진도개와 삽사리 혈액 단백질의 비교연구 II. 혈청 Lactate Dehydrogenase와 혈청 Alkaline Phosphatase의 동위효소와 활성도

  • 김종봉;윤인숙
    • 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.

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Genetic Analysis of Esterase Isozymes in Tillering Maize (분벽성 옥수수에 대한 Esterase 동위효소의 유전분석)

  • 이희봉
    • KOREAN JOURNAL OF CROP SCIENCE
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    • v.35 no.2
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    • pp.146-150
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    • 1990
  • This study was conducted to investigate the genetic analysis of esterase isozymes in maize with tillers. The materials used for the study were stele tissue for five day old seedlings of IK inbred line with tiller and A-type inbred line with no tiller, their Fl and F,. The methods employed for the study were same as previous report by Lee and Choe. A total of thirteen isoesterase enzyme bands were identified and five zones were distinguised according to both migration distance and genetic segregation patterns. The E$\sub$0.3/, E$\sub$0.4/ and E$\sub$0.5/ loci appeared from orgin to 0.5cm migration distance were controlled by the two alleles in (IK/A-type)F$_2$ and the E$\sub$0.3/+E$\sub$0.4/ of variants was controlled by codominant alleles. The E$\sub$1.0/, E$\sub$1.2/, E$\sub$1.5/ and E$\sub$1.8/ loci appeared from 1.0cm to 1.8cm were also controlled by the two alleles. However, the null band was functioned alleles. The E$\sub$2.8/, E$\sub$3.0/ and E$\sub$3.5/ loci appeared from 2.8cm to 3.5cm migration distance were very active and near location. A total of individuals with two paried bands of these loci were more than those of three paired bands(x$^2$=0.327$\^$**/). The activity of bands appeared over 3.8cm were very low and these were controlled by the two alleles. In above results, genetic segregations of stele tissue of maize with tillers were suggested to be controlled by Mendelian genetic laws.

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