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glutamate dehydrogenase and Na^+-K^+ ATPase expression and growth response of Litopenaeus vannamei to different salinities and dietary protein levels

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Chinese Journal of Oceanology and Limnology 2011年第2期29卷 343-349页

作者：李二超 Leticia ARENA Gabriel LIZAMA Gabriela GAXIOLA Gerard CUZON Carlos ROSAS 陈立侨 Alain VAN WORMHOUDT School of Life Science East China Normal University UMR5178 Station de Biologie Marine du Musum National d'Histoire NaturelleBP225Concarneau 29900France Unidad Multidisciplinaria de Docencia e Investigación Facultad de CienciasUniversidad Nacional Autónoma de MxicoPuerto de abrigo s/nSisal C.P.97350HunucmYucatnMexico IFREMER TahitiFrench Polynesia

Improvement in the osmoregulation capacity via nutritional supplies is vitally important in shrimp *** effects of dietary protein levels on the osmoregulation capacity of the Pacific white shrimp(***) were *** involved an examination of growth performance,glutamate dehydrogenase(GDH) and Na+-K+ ATPase mRNA expression,,and GDH activity in muscles and *** experimental diets were formulated,containing 25%,40%,and 50% dietary protein,and fed to the shrimp at a salinity of *** 20 days,no significant difference was observed in weight gain,though GDH and Na+-K+ ATPase gene expression and GDH activity increased with higher dietary protein ***,shrimp fed diets with 25% and 50% dietary protein were transferred into tanks with salinities of 38 and 5,respectively,and sampled at weeks 1 and *** fed with 40% protein at 25 in salinity(optimal conditions) were used as a *** of the salinities,shrimp fed with 50% dietary protein had significantly higher growth performance than other diets;no significant differences were found in comparison with the *** fed with 25% dietary protein and maintained at salinities of 38 and 5 had significantly lower weight gain values after 2 *** salinity change also stimulated the hepatosomatic index,which increased in the first week and then recovered to a relatively normal level,as in the control,after 2 *** findings indicate that in white shrimp,the specific protein nutrient and energy demands related to ambient salinity change are associated with protein *** dietary protein level could improve the osmoregulation capacity of *** with more energy resources allocated to GDH activity and expression.

关键词： Litopenaeus vannamei gene expression glutamate dehydrogenase Na^+-K^+ ATPase protein salinity

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Involvement of the ammonium assimilation mediated by glutamate dehydrogenase in response to heat stress in the scleractinian coral Pocillopora damicornis

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Journal of Oceanology and Limnology 2022年第5期40卷 2001-2011页

作者： Jia TANG Wenqi CAI Zhicong YAN Zhongjie WU Qianxi YANG Zhi ZHOU State Key Laboratory of Marine Resource Utilization in South China Sea Key Laboratory of Tropical Hydrobiology and Biotechnology of Hainan ProvinceHainan Aquaculture Breeding Engineering Research CenterHainan UniversityHaikou 570228China Hainan Academy of Ocean and Fisheries Sciences Haikou 570228China

glutamate dehydrogenase(GDH)plays an important role in the ammonium assimilation and nitrogen metabolism by catalyzing the reversible oxidative deamination of L-glutamate toα-*** the present study,the potential functions of GDH in response to heat stre ss were explored in the scleractinian coral Pocillopora damicornis(designated as PdGDH).The cDNA of PdGDH contained an open reading frame of 1611 bp encoding a polypeptide of 536 amino acids,which exhibited the highest sequence identity to GDH of Stylophora pistillata(96%identity),and the deduced PdGDH protein was predicted to contain one GdhA domain(from Val95 to Tyr525).The recombinant protein of PdGDH(rPdGDH)was expressed in Escherichia coli BL21(DE3)-Transetta,and its catalytic activity was measured under different temperatures,pH conditions and epigallocatechin-3-gallate(EGCG,a GDH inhibitor)*** purified rPdGDH only used reduced coenzyme nicotinamide adenine dinucleotide(NADH)as coenzyme,and its highe st activity was observed at 35℃and pH 7.5,re *** rPdGDH activity was negatively correlated with the concentration of EGCG,and was inhibited by more than half(65%,P0.05).Furthermore,the activities of NADH-GDH in the scleractinian coral *** increased significantly at 12 h after the heat and ammonium stress,and the NADH-GDH activity in the heat stress group(32.66 U/mg,Pglutamate dehydrogenase in the scleractinian coral ***,could respond to heat stress at the protein level,which would have ability to further promote ammonium assimilation to increase the heat acclimatization of the coral-Symbiodiniaceae symbiotic association.

关键词： scleractinian coral glutamate dehydrogenase ammonium assimilation global warming heat response

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Effect of Exogenous Ammonium on GlutamineSynthetase, glutamate Synthase, and glutamate dehydrogenase in the Root of Rice Seedling

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Wuhan University Journal of Natural Sciences 1999年第3期4卷 358-362页

作者： Li, Ze-song Zhang, Chu-fu Lin, Qing-hua Peng, Jin Li, Chang-jian He, Guang-cun Peng, Shao-bing John, Bennett

Root biomass of rice seedlings was increased at lower concentration of exogenous NH 4 + , but it was decreased at higher concentration of exogenous NH 4 + . The level of free NH 4 + in the roots was accumulated gradually with the increase of NH 4 + concentration in the nutrient solution. The content of the soluble proteins was essentially constant at higher NH 4 + . The activities of glutamine synthetase (GS), NADH-dependent glutamate synthase (NADH-GOGAT), and NADH-dependent glutamate dehydrogenase (NADH-GDH) were risen with exogenous NH 4 + concentration at the lower NH 4 + concentration range. But the activities of GS and NADH-GOGAT were declined, and the level of NADH-GDH activity was kept constant under higher NH 4 + concentration. The GS/GDH ratio suggested that NH 4 + was assimilated by GS-GOGAT cycle under lower NH 4 + concentration, but NADH-GDH was more important for NH 4 + assimilation and detoxifying NH 4 + to the tissue cells at the higher NH 4 + level. According to the growth and the activity changes of these ammonium-assimilating enzymes of rice seedling roots, 10. 0 μg/mL NH 4 + -N in nutrient solution was more suitable to the rice growth.

关键词： ammonium glutamine synthetase glutamate synthase glutamate dehydrogenase rice root

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Research on glutamate dehydrogenase Activity in Sugar Beet (Beta vulgaris L) under Different Nitrogen Levels

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Journal of Northeast Agricultural University(English Edition) 1998年第2期5卷 117-121页

作者： Yan Guiping, Li Wenhua and Ma Fengming (Northeast Agricultural University, Harbin 150030, P R C)

The experiment of glutamate dehydrogenase (GDH) activity in various plant parts under different nitrogen levels in frame culture during the whole period of growth was carried out on campus of Northeast Agricltural University in 1993. The result showed that GDH activity in leaf blades under four nitrogen applied levels rose rapidly to the acme from the seedling to foliage rapid growth stage, then diminished rapidly to the lower level at the latter stage of foliage rapid growth. This level was kept to harvest. GDH activity in roots at each growth stage under all nitrogen levels exhibited little disparity and did not show ostensible regularity of changes. GDH activity in leaf blades was stimulated with nitrogen, however, it reduced with nitrogen fertilizer applying further. GDH activity in leaf blades was the biggest compared with crowns, petioles and roots, which suggested that it could represent the highest enzyme activityof the whole plant.

关键词： sugar beet nitrogen level glutamate dehydrogenase

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Purification and characterization of a thermostable glutamate dehydrogenase from a thermophilic microorganism from Deception Island, Antarctica

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Advances in Polar Science 2016年第1期27卷 8-13页

作者： Patricio A. Flores M. Freddy Boehmwald Jenny M. Blamey A. Fundacion Cientifica y Cultural Biociencia Santiago Chile Jose Domingo Cafias 2280 Santiago Chile 775-0132 Universidad de Santiago Santiago Chile

glutamate dehydrogenase （GDH） catalyzes the oxidative deamination of glutamate to a-ketoglutarate and ammonium ions. Currently the determination of ammonium and glutamate is carried out using a bovine GDH enzyme, which lacks optimal thermostability for long term storage at room temperature. From samples of Deception Island, Antarctica, we obtained the thermophilic bacteria PID 15 belonging to the Bacillus genera with high GDH specific activity. This new enzyme exhibited NAD＋ dependent activity and no activity was observed when NADP＋ was used. This enzyme shows a specific activity of 4.7 ***-1 for the oxidative deamination reaction and 15.4 U·mg-1 for the reduction of a-ketoglutarate. This enzyme has an optimum temperature of 65℃ and pH of 8.5 for the oxidative deamination. For the reduction of a-ketoglutarate, the optimum temperature is 60℃, with a pH of 8.0. One of the most important characteristics of this enzyme is its ability to retain more than 60% of its activity when it is incubated for 8 h at 65℃. The enzyme is also able to retain full activity when it is incubated for 48 d at 4℃ and over 80% of its activity when it is incubated at 25℃. Characterization of its kinetics suggests that it primarily catalyzes the formation of α-ketoglutarate. This enzyme has an important biological role in the catabolism of glutamate and may have some interesting biotechnological applications based on its thermostable properties.

关键词： Antarctica glutamate dehydrogenase thermophile

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The Role of glutamate dehydrogenase Activity in Development of Neurodegenerative Disorders

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World Journal of Neuroscience 2017年第1期7卷 181-192页

作者： Matej Kravos Ivan Malesic University of Litoral KoperSlovenia Faculty of Medicine University of MariborMariborSlovenia

The specific role of glutamate dehydrogenase (GLDH) in the brain is not yet clear, but it is an important enzyme in protein degradation as well as a metabolism regulator of glutamate as a neurotransmitter. The enzyme probably provides crucial protection for postsynaptic membranes against the neurotoxic effects of glutamate neurotransmitters. In men, GLDH activity declines almost evenly through the ages;in women, it declines faster in the first five decades. In the years of menopause, GLDH activity declines slower. The diminished GLDH activities in leukocytes and in the brain vary considerably, but they are parallel with the progress of neurodegenerative diseases. The GLDH activity is partly deficient in the brain, particularly in the leukocytes of patients with heterogeneous neurological disorders and degeneration of multiple neuronal systems. We found a statistically significant difference of GLDH activity in the cerebrospinal fluid in patients with neurological diseases and unexpected in patients with degenerative and inflammatory disorders. The decrease in GLDH activity in the cerebrospinal fluid of patients with neurodegenerative disorders may be one of the reasons for the neuro-excito-toxic glutamate effect. Defining the GLDH activity in leukocytes is at the moment the sole experimental method. The second one could be the measurement in cerebrospinal fluid. The results suggest a possibility to regulate glutamate level in human brain through activation of GLDH.

关键词： glutamate dehydrogenase Neurodegenerative Disorders Leukocyte GLDH Cerebrospinal Fluid GLDH

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Prokaryotic Expression of Gene Encoding glutamate dehydrogenase of Streptococcus suis Serotype 2 and Preparation of Polyclonal Antibodies against Its Expressed Products

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Animal Husbandry and Feed Science 2011年第5期3卷 15-19页

作者： XIA Xiao-jing SHEN Zhi-qiang JIANG Shi-jin LI Shu-guang WU Li-zhi MA Zhen-qian CHENG Li-kun College of Animal Science & Veterinary Medicine Shandong Agricultural University Taian 271018 China Shandong Binzhou Animal Science & Veterinary Medicine Academy Binzhou 256600 China Shandong Lvdu Biotechnology Co. Ltd. Binzhou 256600 China College of Animal Science and Technology Huazhong Agricultural University Wuhan 430070 China College of Animal Science and Veterinary Medicine Shenyang Agricultural University Shenyang 110161 China

[ Objective] To obtain detection antigen for diagnosis of Streptococcus suis infection. [ Method] The complete ORF of glutamate dehy- drogenase （GDH） gene was amplified from the genomic DNA of Streptococcus suis serotype 2 strain SC22 isolated in Sichuan Province by poly- merase chain reaction （PCR）. The resulting product was cloned into the prokaryotic expression vector pET-30a, which was then transformed into E. coil BL21 （DE3）. The identified positive transformants were screened for expression induced by IPTG. The expression products were subjected to SDS-PAGE and the recombinant protein was purified by nickel ion-agarose affinity chromatography. New Zealand rabbits were immunized with the purified recombinant GDH protein to prepare polyclonal antibodies. Titers of the anti-serum were determined by indirect ELISA and Western blot assay. [ Result] The recombinant GDH protein was effectively expressed in the host bacteria, and highly pure recombinant protein was obtained by nickel ion-agarose affinity chromatography. High-titer anti-serum against the recombinant protein was obtained. As evidenced by western blot as- say, the sera could react specifically with the lysates of all detected Streptococcus suis strains. In addition, the recombinant GDH protein could re- act specifically with serum samples collected from five pigs experimentally infected by strain SC22. [ Conclusion] The expressed GDH fusion protein has some common epitopes of natural GDH and can be used as detection antigen to develop ELISA and other diagnostic methods.

关键词： Streptococcus suis serotype 2 glutamate dehydrogenase Prokaryotic expression Western blot

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NADH-dependent glutamate dehydrogenase(PoGDH) of Pleurotus ostreatus exhibits higher aminating activities in vitro

NADH-dependent glutamate dehydrogenase(PoGDH) of Pleurotus o...

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多彩菌物美丽中国——中国菌物学会2019年学术年会

作者：文晴安运平胡越朱琳张少康申进文河南农业大学生命科学学院

Nitrogen, an essential macronutrient for edible fungi growth and development, is assimilated by the glutamine synthetase/glutamate synthase(GS/GOGAT) cycle or glutamate dehydrogenase(GDH) pathway in microorganism. GDH, which catalyzes the reversible conversion between glutamate and α-ketoglutarate, plays a crucial role in coupling of carbon and nitrogen metabolism in organism. Overexpression of GDH gene can improve the abilities of nitrogen assimilation and stress tolerance of plants. A putative GDH coding gene,designated as PoGDH, was isolated from P. ostreatus. The bioinformatics analysis showed that PoGDH protein shared high similarity with NAD[H]-dependent glutamate dehydrogenase(NAD[H]-GDH) from other organisms,and the optimal coenzyme of PoGDH was NADH as we determined. The biochemical analysis showed that the Mw of monomer and polymer of PoGDH were separately 117 k Da and 700 k Da, which indicates that the native PoGDH is homohexamer as expected. The Km value of PoGDH for ammonium, α-ketoglutarate and glutamate were separately 2.953 m M, 0.184 m M and 0.318 m M, and the Kcat/Km ratio of PoGDH for ammonium,α-ketoglutarate and glutamate were separately 5503, 4982 and 4168 m M S. The above results reveal that PoGDH has higher affinity to α-ketoglutarate and mainly catalyzes the reductive amination of α-ketoglutarate in vitro.

关键词： Pleurotus ostreatus Nitrogen metabolism glutamate dehydrogenase Prokaryotic expression Homohexamer Reductive amination

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Current knowledge on the laboratory diagnosis of Clostridium difficile infection

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World Journal of Gastroenterology 2017年第9期23卷 1552-1567页

作者： Adrián Martínez-Meléndez Adrián Camacho-Ortiz Rayo Morfin-Otero Héctor Jesús Maldonado-Garza Licet Villarreal-Trevino Elvira Garza-González Departamento de Microbiología e Inmunología Facultad de Ciencias BiológicasUniversidad Autónoma de Nuevo León.Pedro de Alba S/NCiudad UniversitariaSan Nicolás de los Garza Servicio de Infectología Hospital Universitario“Dr.JoséEleuterio González”Universidad Autónoma de Nuevo León.Av.Francisco I.Madero Pte.S/NCol.Mitras Centro.Monterrey Hospital Civil de Guadalajara “Fray Antonio Alcalde”e Instituto de Patología Infecciosa y ExperimentalCentro Universitario de Ciencias de la SaludUniversidadde Guadalajara.Sierra Mojada 950Col.Independencia Servicio de Gastroenterología Hospital Universitario“Dr.JoséEleuterio González”Universidad Autónoma de Nuevo León.Av.Francisco I.Madero Pte.S/NCol.Mitras Centro.Monterrey

Clostridium difficile (C. difficile) is a spore-forming, toxin-producing, gram-positive anaerobic bacterium that is the principal etiologic agent of antibiotic-associated diarrhea. Infection with C. difficile (CDI) is characterized by diarrhea in clinical syndromes that vary from selflimited to mild or severe. Since its initial recognition as the causative agent of pseudomembranous colitis, C. difficile has spread around the world. CDI is one of the most common healthcare-associated infections and a significant cause of morbidity and mortality among older adult hospitalized patients. Due to extensive antibiotic usage, the number of CDIs has increased. Diagnosis of CDI is often difficult and has a substantial impact on the management of patients with the disease, mainly with regards to antibiotic management. The diagnosis of CDI is primarily based on the clinical signs and symptoms and is only confirmed by laboratory testing. Despite the high burden of CDI and the increasing interest in the disease, episodes of CDI are often misdiagnosed. The reasons for misdiagnosis are the lack of clinical suspicion or the use of inappropriate tests. The proper diagnosis of CDI reduces transmission, prevents inadequate or unnecessary treatments, and assures best antibiotic treatment. We review the options for the laboratory diagnosis of CDI within the settings of the most accepted guidelines for CDI diagnosis, treatment, and prevention of CDI.

关键词： Clostridium difficile Toxigenic culture Nucleic acid amplification tests Enzyme immunoassay Diagnosis glutamate dehydrogenase

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Differential Effect of Aluminium on Enzymes of Nitrogen Assimilation in Excised Bean Leaf Segments

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Advances in Biological Chemistry 2016年第3期6卷 106-113页

作者： Priyanka Gupta Juliana Sarengthem Sonal Dhamgaye Rekha Gadre School of Biochemistry Devi Ahilya University Indore India

Aluminium is a potent toxicant in acidic soils. The present study was taken up to analyze the effects of Al on enzymes of nitrogen assimilation in excised bean (Phaseolus vulgaris) leaf segments so as to gain an insight of the mechanism involved. Supply of 0.001 to 0.1 mM AlCl3 to excised bean leaf segments affected the in vivo nitrate reductase activity differently in the presence of various inorganic nitrogenous compounds, being inhibited with 5 mM ammonium nitrate and 10 mM ammonium chloride but enhanced with 10 mM potassium nitrate. Al effect with 50 mM KNO3 varied with time, showing an increased activity at shorter duration, but decreased at longer duration. Al effect on in vivo NRA was dependent upon the nitrate concentration, thus, inhibiting it at 0, 1 and 50 mM KNO3, while increasing at 2 and 10 mM. Further, saturating and non-saturating effects were observed in the absence and presence of Al. Al supply influenced the in vitro NRA also, being increased at 10 mM, but decreased at 50 mM KNO3. Supply of Al to excised leaf segments substantially inhibited the glutamate dehydrogenase activity in the absence as well as presence of 5 mM NH4NO3 but increased the glutamate synthase activity. Inhibition of specific glutamate dehydrogenase activity by Al supply was also observed. However, specific glutamate synthase activity was increased in the presence of NH4NO3 only. The experiments demonstrated that effect of supply of aluminium on in vivo nitrate reductase activity depended upon nitrogenous source as well as nitrate concentration and it exerted reciprocal regulation of glutamate dehydrogenase and glutamate synthase activities, which depended upon N supply too.

关键词： Aluminium Effects glutamate dehydrogenase glutamate Synthase Nitrate Reductase Bean Leaves Phaseolus vulgaris

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