• 제목/요약/키워드: Malate Dehydrogenase

검색결과 131건 처리시간 0.027초

느타리버섯과 잔나비걸상버섯과의 이목간(異目間) 원형질체(原形質體) 융합(融合) (Interorder Protoplast Fusion between Pleurotus ostreatus and Ganoderma applanatum)

  • 유영복;송문태;고승주;유창현;차동열;박용환;장권열
    • 한국균학회지
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    • 제17권3호
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    • pp.119-123
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    • 1989
  • 주름버섯목(目) 느타리버섯과 민주름버섯목(目) 잔나비걸상버섯과의 이목간(異目間) 원형질체(原形質體)를 polyethylene glycol로 유도하여 융합주(融合株) heterokaryon을 선발하였다. 버섯최소배지에서 극히 균사생장이 느렸으며 버섯완전배지에서 3번 계대배양되면서 다소 생장이 빨라졌다. 융합주 36균주의 75%는 양친의 균사가 혼합된 균총형태였으며 16.7%는 새로운 형태, 8.3%는 느타리버섯 형태이었다. 이들 중 양친의 균총(菌叢)이 혼합된 형태는 3번 계대배양 후 모두 느타리버섯 형태로 변하였다. 균사(菌絲)에는 클램프연결체가 없었고 원기(原基)도 형성하지 않았다. 융합주(融合株)를 전기영동법으로 esterase, malate dehydrogenase, peroxidase의 동위효소(同位酵素) 분석(分析)으로 비교하였는데 잔나비걸상버섯 효소는 뚜렷하지 않았으나 새로운 밴드의 형성으로 보아 두 양친 genome간의 상호작용이 존재하였다.

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고온에 의한 변색단계별 '홍로' 사과의 착색 및 당 축적 관련 유전자 발현 분석 (Expression of Genes Affecting Skin Coloration and Sugar Accumulation in 'Hongro' Apple Fruits at Ripening Stages in High Temperatures)

  • 김선애;안순영;윤해근
    • 생물환경조절학회지
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    • 제25권1호
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    • pp.9-15
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    • 2016
  • 고온은 사과(Malus domestica Borkh) 과실의 품질에 영향을 끼치는 가장 중요한 환경 요인 중 하나이다. 착색기의 '홍로' 사과 과실을 3단계로 구분하여 Real-time PCR을 통해 온도조건에 따른 안토시아닌 합성과 당 축적 관련 유전자의 발현 차이를 조사하였다. 당 합성관련 유전자인 ${\beta}$-amylase(BMY)와 polygalacturonase(PG)의 발현은 변색 시작단계보다 마지막 단계에서 월등히 높았다. 과피의 착색과 관련있는 phenylalanine ammonia-lyase(PAL), chalcone synthase(CHS), flavanone 3-hydroxylase(F3H)와 malate dehydrogenase(MDH)유전자는 변색 초기작단계에서는 고온 처리 24시간후에 발현이 증가하는 경향을 보였으며 변색 중간단계에서는 점차 증가하는 경향을 보였다. 변색단계별로 보았을 때 $25^{\circ}C$처리구가 다른 온도처리구보다 발현 정도가 더 높았으며, 변색 시작단계보다 마지막 단계에서의 발현이 강하게 유도되었다. 본 연구의 결과로 착색 초기단계의 과실이 고온스트레스가 가장 영향을 끼치므로 착색초기단계의 과실을 이용하여 전사체를 분석하면 분자생물학적 수준에서 사과의 성숙대사에서 유용한 정보를 얻을 수 있을 것으로 사료된다.

과채류 시설재배지 식물기생선충 분포 및 효소표현형을 이용한 뿌리혹선충의 동정 (Distribution of Plant-parasitic Nematodes in Fruit Vegetable Production Areas in Korea and Identification of Root-knot Nematodes by Enzyme Phenotypes)

  • 조명래;이봉춘;김동순;전흥용;임명순;이정운
    • 한국응용곤충학회지
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    • 제39권2호
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    • pp.123-129
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    • 2000
  • 국내 과채류 재배단지의 뿌리혹선충 발생에 관한 조사를 위해 1997년부터 1999년까지 경북 성주군을 중심으로 경기 여주군, 경남 함안군, 충북 청원군 등에서 과채류재배지의 토양을 채집하여 식물기생선충 종류와 밀도 조사, 뿌리혹선충 암컷의 효소표현형에 의한 종 동정을 실시하였다. 경북 성주군의 185개 참외재배 포장 중 99개 포장(53.5%)에서 뿌리혹선충이 검출되었고 나선선충류(Helocotylenchus spp.)는 7개, 둥근꼬리선충류(Aphelechus spp.)는 43개, 환선충류(Criconematid)는 26개 포장에서 검출되었다. 뿌리혹선충 암컷의 Malate dehydrogenase 및 Esterase 등 2가지 효소표현형을 이용하여 한국에 분포하는 주요 4종의 동정이 가능하였다. 효소 표현형을 이용하여 성주군 선남면에서 채집된 13개 시료 중 당콩뿌리혹선충으로 동정된 것이 6포장, 고구마뿌리혹선충 5포장이었으며 2개 포장은 두 종의 혼재하는 것으로 나타났다. 성주군 초전면의 6개 포장 시료 중 4개가 땅콩뿌리혹선충, 1개가 고구마뿌리혹선충으로 동정되었으며 1포장의 뿌리혹선충은 효소표현형이 미동정 종으로 나타났다. 경기도 여주군의 참외재배단지에서는 14개 조사대상 중 당근뿌리혹선충이 11개 포장, 땅콩뿌리혹선충이 3개포장으로 당근뿌리혹선충이 우점종인 것으로 나타났다.

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Fusarium속 내의 section Elegans, section Liseola와 유사종의 Isozyme Patterns (Isozyme patterns of section Elegans, section Liseola and similar species in the genus Fusarium)

  • 민병례;권오영
    • 한국균학회지
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    • 제22권4호
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    • pp.386-393
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    • 1994
  • Fusarium 속내 종들의 분류학적 위치를 알아보기 위하여, 각 균의 $esterase-{\alpha},\;-{\beta},\;acid\;phosphatase,\;malate\;dehydrogenase,\;peroxidase,\;polygalacturonase$를 추출하여 전기영동의 방법으로 isozyme patterns를 비교하여 보았다. Banding patterns은 polygalacturonase만이 7종 모두에서 monozyme이었고, 나머지 효소는 종마다 약간씩 다르게 나타났다. Isozyme banding patterns을 바탕으로 genetic similarity를 산출하여 dendrogram으로 보았을 때, 동일한 section Liseola에 속하는 F. subglutinans와 F. moniliforme의 종간 유사도는 74.3%로 가장 높았으며, section Elegans와 section Liseola의 서로 다른 section 간의 유사도는 45.4%로 비교적 낮았다. F. napiforme와 F. nygamai의 유사도는 64.7%로 동일 section 내의 종간 유사도와 비슷한 수치를 나타내었다. 이들 두 종은 section Liseola에 대하여 55.2%, section Elegans에 대하여 45.4%의 유사도를 보여 분류학적 위치에 있어서 section Liseola에 더 가까운 경향을 나타내지만, 이는 다른 section 간의 유사도와 비슷한 수치로 하나의 독립된 section으로 추정된다. F. graminearum과 다른 6종 사이의 유사도는 28.2%의 낮은 수치를 나타내어 서로의 유사성이 매우 낮다는 것을 보여 주었다.

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잡초종(雜草種)에 대한 Paraquat 독성(毒性) : 내성종(耐性種)과 감수성(感受性) 종간(種間)의 반응(反應) 차이(差異) (Paraquat Toxicity in Weed Species : Difference in Physiological Responses between Tolerant and Susceptible Species)

  • 강병화;심상인
    • 한국잡초학회지
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    • 제15권3호
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    • pp.224-231
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    • 1995
  • Paraquat에 대한 잡초종(雜草種)의 다양한 반응(反應)은 여러 가지 요인에 의한다. Paraquat에 대하여 내성종(耐性種)과 감수성종(感受性種)은 가시적(可視的)인 피해율(被害率)의 차이(差異)를 비롯하여 체내(體內) 물질(物質) 변화(變化)의 차이(差異)는 물론 체내(體內) 효소(酵素) 활성(活性)의 차이(差異) 등을 나타났다. 내성종(耐性種)은 paraquat에 의한 photosystem II의 활성(活性) 저하(低下) 정도가 감수성종(感受性種)보다 작았으며, 지질(脂質)의 과산화(過酸化) 정도(程度) 역시 내성종(耐性種)에서 낮았다. 체내(體內) 물질(物質) 중 엽록소(葉綠素)는 paraquat에 의해 줄어들었으나 환원당(還元糖)의 경우는 paraquat의 농도(濃度)가 높아질수록 증가하였다. 항산화제(抗酸化劑)인 glutathione의 경우 처리농도(處理濃度)가 증가함에 따라 함량(含量)이 증가하는 경향이었으나 내성종(耐性種)과 감수성종(感受性種)의 구분은 뚜렷하지 않았다. 항산화효소(抗酸化酵素)인 glutathione reductase의 활성(活性)은 내성종(耐性種)에서 높게 나타났으며, superoxide dismutase의 경우는 paraquat의 처리농도(處理濃度)가 증가함에 따라 그 활성(活性)이 증가하였다. 체내대사(體內代謝)의 주요 효소(酵素)들인 catalase, NADPH-cytochrome c reductase, malate dehydrogenase의 활성(活性)은 catalase의 경우 저농도(低濃度)의 paraquat에 의해서는 활성(活性) 저하(低下) 정도(程度)가 낮은 반면 나머지 두 효소(酵素)는 저농도(低濃度)에서부터 급격한 활성저하(活性低下)가 나타났다.

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Comprehensive investigations of key mitochondrial metabolic changes in senescent human fibroblasts

  • Ghneim, Hazem K.;Alfhili, Mohammad A.;Alharbi, Sami O.;Alhusayni, Shady M.;Abudawood, Manal;Aljaser, Feda S.;Al-Sheikh, Yazeed A.
    • The Korean Journal of Physiology and Pharmacology
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    • 제26권4호
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    • pp.263-275
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    • 2022
  • There is a paucity of detailed data related to the effect of senescence on the mitochondrial antioxidant capacity and redox state of senescent human cells. Activities of TCA cycle enzymes, respiratory chain complexes, hydrogen peroxide (H2O2), superoxide anions (SA), lipid peroxides (LPO), protein carbonyl content (PCC), thioredoxin reductase 2 (TrxR2), superoxide dismutase 2 (SOD2), glutathione peroxidase 1 (GPx1), glutathione reductase (GR), reduced glutathione (GSH), and oxidized glutathione (GSSG), along with levels of nicotinamide cofactors and ATP content were measured in young and senescent human foreskin fibroblasts. Primary and senescent cultures were biochemically identified by monitoring the augmented cellular activities of key glycolytic enzymes including phosphofructokinase, lactate dehydrogenase, and glycogen phosphorylase, and accumulation of H2O2, SA, LPO, PCC, and GSSG. Citrate synthase, aconitase, α-ketoglutarate dehydrogenase, succinate dehydrogenase, malate dehydrogenase, isocitrate dehydrogenase, and complex I-III, II-III, and IV activities were significantly diminished in P25 and P35 cells compared to P5 cells. This was accompanied by significant accumulation of mitochondrial H2O2, SA, LPO, and PCC, along with increased transcriptional and enzymatic activities of TrxR2, SOD2, GPx1, and GR. Notably, the GSH/GSSG ratio was significantly reduced whereas NAD+/NADH and NADP+/NADPH ratios were significantly elevated. Metabolic exhaustion was also evident in senescent cells underscored by the severely diminished ATP/ADP ratio. Profound oxidative stress may contribute, at least in part, to senescence pointing at a potential protective role of antioxidants in aging-associated disease.

Proteomic Analysis of Bovine Muscle Satellite Cells during Myogenic Differentiation

  • Rajesh, Ramanna Valmiki;Jang, Eun-Jeong;Choi, In-Ho;Heo, Kang-Nyeong;Yoon, Du-Hak;Kim, Tae-Hun;Lee, Hyun-Jeong
    • Asian-Australasian Journal of Animal Sciences
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    • 제24권9호
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    • pp.1288-1302
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    • 2011
  • The aim of this study was to analyze the proteome expression of bovine satellite cells from longissimus dorsi (LD), deep pectoral (DP) and semitendinosus (ST) muscle depots during in vitro myogenic differentiation. Proteomic profiling by twodimensional gel electrophoresis and mass spectrometry of differentiating satellite cells revealed a total of 38 proteins that were differentially regulated among the three depots. Among differentially regulated proteins, metabolic proteins like lactate dehydrogenase (LDH), malate dehydrogenase (MDH) were found to be up regulated in ST, while alpha-enolase (NNE) in LD and DP depot satellite cells were down regulated. Also, our analysis found that there was a prominent up regulation of cytoskeletal proteins like actin, actincapping protein and transgelin along with chaperone proteins like heat shock protein beta 1 (HSPB 1) and T-complex protein 1 (TCP-1). Among other up regulated proteins, LIM domain containing protein, annexin 2 and Rho GDP-dissociation inhibitor 1 (Rho GDI) are observed, which were already proven to be involved in the myogeneis. More interestingly, satellite cells from ST depot were found to have a higher myotube formation rate than the cells from the other two depots. Taken together, our results demonstrated that, proteins involved in glucose metabolism, cytoskeletal modeling and protein folding plays a key role in the myogenic differentiation of bovine satellite cells.

Cooperativity of ${\alpha}$- and ${\beta}$-Subunits of Group II Chaperonin from the Hyperthermophilic Archaeum Aeropyrum pernix K1

  • Kim, Jeong-Hwan;Lee, Jin-Woo;Shin, Eun-Jung;Nam, Soo-Wan
    • Journal of Microbiology and Biotechnology
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    • 제21권2호
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    • pp.212-217
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    • 2011
  • ${\alpha}$ and ${\beta}$-subunits (ApCpnA and ApCpnB) are group II chaperonins from the hyperthermophilic archaeum Aeropyrum pernix K1, specialized in preventing the aggregation and inactivation of substrate proteins under conditions of transient heat stress. In the present study, the cooperativity of ${\alpha}$- and ${\beta}$-subunits from the A. pernix K1 was investigated. The ApCpnA and ApCpnB chaperonin genes were overexpressed in E. coli Rosetta and Codonplus (DE3), respectively. Each of the recombinant ${\alpha}$- and ${\beta}$-subunits was purified to 92% and 94% by using anionexchange chromatography. The cooperative activity between purified ${\alpha}$- and ${\beta}$-subunits was examined using citrate synthase (CS), alcohol dehydrogenase (ADH), and malate dehydrogenase (MDH) as substrate proteins. The addition of both ${\alpha}$- and ${\beta}$-subunits could effectively protect CS and ADH from thermal aggregation and inactivation at $43^{\circ}C$ and $50^{\circ}C$, respectively, and MDH from thermal inactivation at $80^{\circ}C$C and $85^{\circ}C$. Moreover, in the presence of ATP, the protective effects of ${\alpha}$- and ${\beta}$-subunits on CS from thermal aggregation and inactivation, and ADH from thermal aggregation, were more enhanced, whereas cooperation between chaperonins and ATP in protection activity on ADH and MDH (at $85^{\circ}C$) from thermal inactivation was not observed. Specifically, the presence of both ${\alpha}$- and ${\beta}$- subunits could effectively protect MDH from thermal inactivation at $80^{\circ}C$ in an ATP-dependent manner.

Proteome analysis of sorghum (Sorghum bicolor L.) leaf in response to waterlogging stress

  • Yun, Min-Heon;Park, Hyeong-Jun;Jeong, Hae-Ryong;Roy, Swapan Kumar;Kwon, Soo Jeong;Chun, Hyen Chung;Cho, Seong-Woo;Woo, Sun-Hee
    • 한국작물학회:학술대회논문집
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    • 한국작물학회 2017년도 9th Asian Crop Science Association conference
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    • pp.119-119
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    • 2017
  • Growth related to morphological and proteome response under waterlogging stress in sorghum has not yet been elucidated. Understanding how plants respond to waterlogging, the present study was conducted in seedlings leaf of the Nam-pung chal cultivar. Regarding 3-leaf stage of sorghum, stem length and plant height were slightly decreased in the treatments during ten days of waterlogging, and chlorophyll contents were also significantly different from 7 days of waterlogging treatment. The results observed from the present study were considered to be influenced by the waterlogging stress more in the $5^{th}$ leaf stage of the growth period of the sorghum, and as the waterlogging treatment progressed, the waterlogging stress gradually influenced the growth difference between the control and the treatment respectively. Using 2-DE method, a total of 74 differentially expressed protein spots were analyzed using LTQ-FT-ICR MS. Of these proteins, 45 proteins were up-regulated in the treatment group, and 32 proteins were down-regulated. Analysis of LTQ-FI-ICR MS showed that about 50% of the proteins involved in carbohydrate metabolic process, metabolic process, and cellular metabolic compound salvage were affected by stress. Malate dehydrogenase protein and Glyceraldehyde-3-phosphate dehydrogenase protein related to carbohydrate metabolic process increased the level of protein expression in both 3 and 5-leaf stage under waterlogging stress. The increased abundance of these proteins may play an active role in response to waterlogging stress. These results provide new insights into the morphological alteration and modulation of differentially expressed proteins in sorghum cultivar.

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Metabolic Elasticity and Induction of Heat Shock Protein 70 in Labeo rohita Acclimated to Three Temperatures

  • Das, T.;Pal, A.K.;Chakraborty, S.K.;Manush, S.M.;Chatterjee, N.;Apte, S.K.
    • Asian-Australasian Journal of Animal Sciences
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    • 제19권7호
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    • pp.1033-1039
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    • 2006
  • The metabolic response of Labeo rohita to thermal acclimation was assessed. Advanced fingerlings of L. rohita (average weight $31{\pm}1.4g$) were acclimated to 31, 33 and $36^{\circ}C$ compared with ambient temperatures ($26^{\circ}C$) for 30 days and different enzymes associated with stress response were estimated. Glycolytic enzyme-Lactate dehydrogenase, (LDH, E.C.1.1.1.27), TCA cycle enzyme-Malate dehydrogenase (MDH, E.C.1.1.1.37), Protein metabolizing enzymes-Aspartate amino transferase (AST, E.C.2.6.1.1) and Alanine amino transferase (ALT, E.C.2.6.1.2) of liver, gill and muscle, Gluconeogenic enzymes-Fructose 1,6 Bi phosphatase (FBPase, E.C. 3.1.3.11) and Glucose 6 phosphatase (G6Pase, E.C. 3.1.3.9) of liver and kidney were significantly (p<0.05) different with increasing acclimation temperatures. Heat Shock Protein-70 (HSP-70) was expressed in increasing intensity at 31, 33 and $36^{\circ}C$ but was not expressed at $26^{\circ}C$. Results suggest that higher acclimation temperatures enhance metabolism and L. rohita maintains homeostasis between $26-36^{\circ}C$ via an acclimation episode. Such adaptation appears to be facilitated by resorting to gluconeogenic and glycogenolytic pathways for energy mobilization and induction of HSPs.