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Pesquisa : D08.811.682.047.820.496 [Categoria DeCS]
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  1 / 21 LILACS  
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Id: biblio-829668
Autor: Porto, Karla Rejane de Andrade; Motti, Priscilla Rezende; Machado, Alexandre Alves; Roel, Antonia Railda.
Título: In vitro evaluation of the effect of botanical formulations used in the control of Aedes aegypti L. (Diptera: Culicidae) on liver enzymes.
Fonte: Rev. Soc. Bras. Med. Trop;49(6):693-697, Dec. 2016. tab, graf.
Idioma: en.
Resumo: Abstract: INTRODUCTION: Dengue fever is a viral disease transmitted by the Aedes aegypti Linn. (1792) (Diptera: Culicidae) mosquito, which is endemic in several regions of Brazil. Alternative methods for the control of the vector include botanical insecticides, which offer advantages such as lower environmental contamination levels and less likelihood of resistant populations. Thus, in this study, the ability of botanical insecticide formulations to inhibit the activity of the liver enzymes serum cholinesterase and malate dehydrogenase was evaluated. METHODS: Inhibition profiles were assessed using in vitro assays for cholinesterase and malate dehydrogenase activity and quantitated by ultraviolet-visible spectroscopy at 410nm to 340nm. RESULTS Insecticide products formulated from cashew nutshell liquid [A] and ricinoleic acid [B] showed cholinesterase activity levels of 6.26IU/mL and 6.61IU/mL, respectively, while the control level for cholinesterase was 5-12IU/mL. The products did not affect the level of 0.44IU/mL established for malate dehydrogenase, as the levels produced by [A] and [B] were 0.43IU/mL and 0.45IU/mL, respectively. CONCLUSIONS Our findings show that in vitro testing of the formulated products at concentrations lethal to A. aegypti did not affect the activity of cholinesterase and malate dehydrogenase, indicating the safety of these products.
Descritores: Ácidos Ricinoleicos/farmacologia
Inibidores da Colinesterase/farmacologia
Colinesterases/efeitos dos fármacos
Anacardium/química
Inseticidas/farmacologia
Fígado/enzimologia
Malato Desidrogenase/antagonistas & inibidores
-Espectrofotometria Ultravioleta
Técnicas In Vitro
Ácidos Ricinoleicos/isolamento & purificação
Aedes
Insetos Vetores/efeitos dos fármacos
Inseticidas/isolamento & purificação
Limites: Humanos
Animais
Responsável: BR1.1 - BIREME


  2 / 21 LILACS  
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Quevedo, Joäo
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Id: lil-718443
Autor: Ferreira, Gabriela K.; Cardoso, Mariane R.; Jeremias, Isabela C.; Gonçalves, Cinara L.; Freitas, Karolina V.; Antonini, Rafaela; Scaini, Giselli; Rezin, Gislaine T.; Quevedo, João; Streck, Emilio L..
Título: Fluvoxamine alters the activity of energy metabolism enzymes in the brain
Fonte: Rev. bras. psiquiatr;36(3):220-226, Jul-Sep/2014. graf.
Idioma: en.
Resumo: Objective: Several studies support the hypothesis that metabolism impairment is involved in the pathophysiology of depression and that some antidepressants act by modulating brain energy metabolism. Thus, we evaluated the activity of Krebs cycle enzymes, the mitochondrial respiratory chain, and creatine kinase in the brain of rats subjected to prolonged administration of fluvoxamine. Methods: Wistar rats received daily administration of fluvoxamine in saline (10, 30, and 60 mg/kg) for 14 days. Twelve hours after the last administration, rats were killed by decapitation and the prefrontal cortex, cerebral cortex, hippocampus, striatum, and cerebellum were rapidly isolated. Results: The activities of citrate synthase, malate dehydrogenase, and complexes I, II-III, and IV were decreased after prolonged administration of fluvoxamine in rats. However, the activities of complex II, succinate dehydrogenase, and creatine kinase were increased. Conclusions: Alterations in activity of energy metabolism enzymes were observed in most brain areas analyzed. Thus, we suggest that the decrease in citrate synthase, malate dehydrogenase, and complexes I, II-III, and IV can be related to adverse effects of pharmacotherapy, but long-term molecular adaptations cannot be ruled out. In addition, we demonstrated that these changes varied according to brain structure or biochemical analysis and were not dose-dependent. .
Descritores: Encéfalo/efeitos dos fármacos
Metabolismo Energético/efeitos dos fármacos
Fluvoxamina/administração & dosagem
Inibidores de Captação de Serotonina/administração & dosagem
-Antidepressivos/administração & dosagem
Encéfalo/enzimologia
Ciclo do Ácido Cítrico/efeitos dos fármacos
Creatina Quinase/efeitos dos fármacos
Transtorno Depressivo/tratamento farmacológico
Transporte de Elétrons/efeitos dos fármacos
Malato Desidrogenase/efeitos dos fármacos
Ratos Wistar
Limites: Animais
Masculino
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


  3 / 21 LILACS  
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Vasconcelos, Paulo Roberto Leitão de
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Id: lil-711591
Autor: Guimarães Filho, Artur; Cunha, Rodrigo Maranguape Silva da; Vasconcelos, Paulo Roberto Leitão de; Guimarães, Sergio Botelho.
Título: Glutamine and ornithine alpha-ketoglutarate supplementation on malate dehydrogenases expression in hepatectomized rats
Fonte: Acta cir. bras;29(6):365-370, 06/2014. tab, graf.
Idioma: en.
Resumo: PURPOSE: To evaluate the relative gene expression (RGE) of cytosolic (MDH1) and mitochondrial (MDH2) malate dehydrogenases enzymes in partially hepatectomized rats after glutamine (GLN) or ornithine alpha-ketoglutarate (OKG) suplementation. METHODS: One-hundred and eight male Wistar rats were randomly distributed into six groups (n=18): CCaL, GLNL and OKGL and fed calcium caseinate (CCa), GLN and OKG, 0.5g/Kg by gavage, 30 minutes before laparotomy. CCaH, GLNH and OKGH groups were likewise fed 30 minutes before 70% partial hepatectomy. Blood and liver samples were collected three, seven and 14 days after laparotomy/hepatectomy for quantification of MDH1/MDH2 enzymes using the real-time polymerase chain reaction (PCR) methodology. Relative enzymes expression was calculated by the 2-ΔΔC T method using the threshold cycle (CT) value for normalization. RESULTS: MDH1/MDH2 RGE was not different in hepatectomized rats treated with OKG compared to rats treated with CCa. However, MDH1/MDH2 RGE was greater on days 3 (321:1/26.48:1) and 7 (2.12:1/2.48:1) while MDH2 RGE was greater on day 14 (7.79:1) in hepatectomized rats treated with GLN compared to control animals. CONCLUSION: Glutamine has beneficial effects in liver regeneration in rats by promoting an up-regulation of the MDH1 and MDH2 relative gene expression. .
Descritores: Expressão Gênica/efeitos dos fármacos
Glutamina/farmacologia
Hepatectomia/métodos
Regeneração Hepática/efeitos dos fármacos
Malato Desidrogenase/metabolismo
Ornitina/análogos & derivados
-Regeneração Hepática/fisiologia
Modelos Animais
Malato Desidrogenase/genética
Ornitina/farmacologia
Distribuição Aleatória
Ratos Wistar
Reação em Cadeia da Polimerase em Tempo Real
Valores de Referência
Reprodutibilidade dos Testes
Fatores de Tempo
Regulação para Cima
Limites: Animais
Masculino
Tipo de Publ: Estudo de Avaliação
Responsável: BR1.1 - BIREME


  4 / 21 LILACS  
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Id: lil-600653
Autor: Vasconcelos, Paulo Roberto Cavalcante de; Costa Neto, Claudio Duarte da; Vasconcelos, Raquel Cavalcante de; Souza, Pedro Paulo Chaves de; Vasconcelos, Paulo Roberto Leitão; Guimarães, Sérgio Botelho.
Título: Effect of glutamine on the mRNA level of key enzymes of malate-aspartate shuttle in the rat intestine subjected to ischemia reperfusion / Efeito da glutamina sobre o nível de RNA Mensageiro das enzimas-chave do ciclo malato-aspartato no intestino de ratos submetidos à isquemia e reperfusão
Fonte: Acta cir. bras;26(supl.1):26-31, 2011. ilus, graf.
Idioma: en.
Resumo: PURPOSE: To determine the effects of oral L-glutamine (L-Gln) and the dipeptide l-alanyl-glutamine (L-Ala-Gln) upon the activity of the malate-aspartate shuttle in the rat distal small intestine following ischemia and reperfusion. METHODS: Seventy-two Wistar rats (350-400g), were randomized in 2 groups (n = 36): group S (Sham) and Group T (Treatment) and divided into 12 subgroups (n = 6): A-A6, and B1-B6. The subgroups A1-A3 were subjected to sham procedures at 30 and 60 minutes. Thirty minutes before the study, rats were treated with calcium caseinate, 0.5g/Kg (subgroups A1, A4, B1, B4), L-Gln, 0.5g / kg (subgroups A2, A5, B2 and B5) or L-Ala-Gln, 0.75g/Kg (subgroups A3, A6, B3, B6), administered by gavage. Ischemia was achieved by clamping the mesenteric vessels, delimiting a segment of bowel 5 cm long and 5 cm apart from the ileocecal valve. Samples were collected 30 and 60 minutes after start of the study for real-time PCR assay of malate dehydrogenases (MDH1-2) and aspartate-aminotransferases (GOT1-2) enzymes. RESULTS: Tissue MDH and GOT mRNA expression in intestinal samples from rats preconditioned with either L-Gln or L-Ala-Gln showed no significant differences both during ischemia and early reperfusion. CONCLUSION: Activation of the malate-aspartate shuttle system appears not to be the mechanism of glutamine-mediated elevation of glucose oxidation in rat intestine during ischemia/reperfusion injury.

OBJETIVO: Determinar os efeitos da administração oral de L-glutamina (L-Gln) e do dipeptídeo L-alanil-glutamina (L-Ala-Gln) sobre a atividade do ciclo malato-aspartato no intestino delgado distal de ratos após isquemia/reperfusão. MÉTODOS: Setenta e dois ratos Wistar (350-400g) foram randomizados em 2 grupos (n = 36): T grupo S (Sham) e grupo (Tratamento) e distribuídos em 12 subgrupos (n = 6): A-A6, e B1-B6. Os subgrupos A1-A3 foram submetidos a procedimentos "sham" aos 30 e 60 minutos. Trinta minutos antes do estudo, os ratos foram tratados com caseinato de cálcio, 0,5 g/kg (subgrupos A1, A4, B1 e B4), L-Gln, 0,5 g/kg (subgrupos A2, A5, B2 e B5) ou L-Ala -Gln, 0,75g/kg (subgrupos A3, A6, B3, B6), administrado por gavagem. A isquemia foi obtida por pinçamento dos vasos mesentéricos, delimitando um segmento do intestino cinco centímetros de comprimento e 5 cm da válvula ileocecal. Amostras foram coletadas aos 30-60 minutos para ensaio de PCR em tempo real das enzimas malato desidrogenases (MDH1-2), aspartato-aminotransferase (GOT1-2). RESULTADOS: A expressão de MDH e GOT mRNA nas amostras provenientes do intestino delgado de ratos pré-condicionados com L-Gln ou L-Ala-Gln não apresentou diferenças significativas, tanto durante a isquemia como na fase inicial de reperfusão. CONCLUSÃO: Ativação do ciclo malato-aspartato não parece ser o mecanismo de elevação glutamina-mediada da oxidação da glicose no intestino de ratos durante a isquemia / reperfusão.
Descritores: Ácido Aspártico/metabolismo
Glutamina/farmacologia
Intestino Delgado/irrigação sanguínea
Malatos/metabolismo
RNA Mensageiro/sangue
Traumatismo por Reperfusão/prevenção & controle
-Aspartato Aminotransferases/sangue
Aspartato Aminotransferases/genética
Modelos Animais de Doenças
Dipeptídeos/farmacologia
Intestino Delgado/enzimologia
Malato Desidrogenase/sangue
Malato Desidrogenase/genética
Distribuição Aleatória
Ratos Wistar
Reação em Cadeia da Polimerase em Tempo Real
Traumatismo por Reperfusão/enzimologia
Fatores de Tempo
Limites: Animais
Ratos
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


  5 / 21 LILACS  
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Id: lil-556860
Autor: Cisternas, C. D; Compagnucci, M. V; Conti, N. R; Ponce, R. H; Vermouth, N. T.
Título: Protective effect of maternal prenatal melatonin administration on rat pups born to mothers submitted to constant light during gestation
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;43(9):874-882, Sept. 2010. ilus, tab.
Idioma: en.
Resumo: We studied the effects of adverse conditions such as constant light (LL) on the circadian rhythm of malate (MDH, EC 1.1.1.37) and lactate (LDH, EC 1.1.1.27) dehydrogenase activities of the testes of male Wistar rats on postnatal day 28 (PN28), anxiety-like behavior (elevated plus-maze test) at PN60 and sexual behavior at PN120. The rats were assigned to mother groups on day 10 of pregnancy: control (12-h light/dark), LL (light from day 10 to 21 of pregnancy), and LL+Mel (LL and sc injection to the mothers of a daily dose of melatonin, 1 mg/kg body weight at circadian time 12, from day 17 to 21 of pregnancy). LL offspring did not show circadian rhythms of MDH (N = 62) and LDH (N = 63) activities (cosinor and ANOVA-LSD Fisher). They presented a 44.7 percent decrease in open-arm entries and a 67.9 percent decrease in time (plus-maze test, N = 15, P < 0.001, Mann-Whitney U-test and Kruskal-Wallis test), an increase in mounting (94.4 percent), intromission (94.5 percent) and ejaculation (56.6 percent) latencies (N = 12, P < 0.01, Mann-Whitney U-test and Kruskal-Wallis test) and lower numbers of these events (61, 59 and 73 percent, respectively; P < 0.01, N = 12) compared to controls. The offspring of the LL+Mel group presented MDH and LDH circadian rhythms (P < 0.05, N = 50, cosinor and ANOVA-LSD Fisher), anxiety-like and sexual behaviors similar to control. These findings supported the importance of the melatonin signal and provide evidence for the protective effects of hormones on maternal programming during gestation. This protective action of melatonin is probably related to its entrainment capacity, favoring internal coupling of the fetal multioscillatory system.
Descritores: Comportamento Animal/efeitos dos fármacos
Ritmo Circadiano/efeitos dos fármacos
Hidroliases/análise
Malato Desidrogenase/análise
Melatonina/farmacologia
Testículo/enzimologia
-Animais Recém-Nascidos
Ansiedade/prevenção & controle
Comportamento Animal/fisiologia
Ritmo Circadiano/fisiologia
Ratos Wistar
Comportamento Sexual/efeitos dos fármacos
Limites: Animais
Feminino
Masculino
Gravidez
Ratos
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


  6 / 21 LILACS  
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Id: lil-509870
Autor: Ballen, Marcia L. O; Moretto, Vera L; Santos, Maisa P. dos; Gonçalves, Talita S. S; Kawashita, Nair H; Stoppiglia, Luis F; Martins, Maria Salete F; Gomes-da-Silva, Maria Helena G.
Título: Restrição protéica na prenhez: efeitos relacionados ao metabolismo materno / Protein restriction in pregnancy: effects related to dam metabolism
Fonte: Arq. bras. endocrinol. metab;53(1):87-94, fev. 2009. graf, tab.
Idioma: pt.
Resumo: Foram avaliadas as alterações no metabolismo materno durante a prenhez em ratas Wistar, prenhes e não-prenhes, submetidas à restrição protéica, que receberam dietas isocalóricas (15,74 kJ/g), controle ou hipoprotéica (17 por cento versus 6 por cento), distribuídas em quatro grupos (n = 7), quais sejam: controle não-prenhe (CNP) e prenhe (CP) e hipoprotéico não-prenhe (HNP) e prenhe (HP), do 1º ao 18º dia de prenhez. Parâmetros bioquímicos, hormonais e relacionados à síntese de lipídios foram considerados. Utilizou-se ANOVA a duas vias seguido de teste Tukey-HSD e teste t de Student, significância de p < 0,05. A restrição protéica elevou a síntese de lipídios e a atividade da enzima málica (EM) no fígado (FIG) e reduziu a massa ( por cento) e a razão lipí+dio/glicogênio nesse tecido, bem como reduziu a ingestão protéica (total e por cento), o conteúdo ( por cento) de lipídios na glândula mamária (GMA), as proteínas e a albumina séricas, com consequente redução nas massas da placenta e fetos. A prenhez reduziu a proteinemia, a albuminemia, a síntese de lipídios, a atividade da EM, os lipídios e o glicogênio no FIG. Mas elevou a massa corporal final, a massa ( por cento) do tecido adiposo gonadal (GON), do FIG e da GMA, e reduziu a massa ( por cento) da carcaça (CARC), a síntese e o conteúdo de lipídios no GON e, na GMA, o conteúdo de lipídios. A insulinemia elevou-se na prenhez, com glicemia reduzida, caracterizando resistência hormonal. A leptina e a prolactina também se elevaram na prenhez, sendo o aumento maior no HP. A restrição protéica na prenhez modificou o metabolismo materno, alterando a síntese de lipídios no FIG e o perfil hormonal, além de reduzir a massa da placenta e dos fetos.

Metabolism alterations were evaluated in female Wistar rats (dams) during pregnancy. Pregnant and non-pregnant dams submitted to protein restriction, were fed isocaloric (15.74 kJ/g), control or hypoproteic (17 percent vs. 6 percent) diets, and distributed in four Groups (n=7) as follows: non-pregnant control (NPC), pregnant control (PC), non-pregnant hypoproteic (NPH), and pregnant hypoproteic (PH); from Day 1 to Day 18 of pregnancy. Biochemical, hormonal and metabolic parameters related to lipid synthesis were assessed. The two-way ANOVA, followed by Tukey-HSD and Student-t tests were used, with a significance of p< 0.05. Protein restriction elevated lipid synthesis and malic enzyme (ME) activity in the liver, and reduced mass and the lipid/glycogen ratio in this tissue; it also lowered protein ingestion (total and percent), lipid content ( percent) in the mammary gland (MAG), serum proteins and albumin, with consequent reduction of placenta and fetal masses. Pregnancy reduced serum protein and albumin concentrations, lipid synthesis, ME activity, hepatic lipid and glycogen content. However, it increased final body mass; increased relative masses of gonad (GON), liver and MAG; but reduced lipid synthesis and content of GON, lipid content of MAG and the relative mass of carcass. Pregnancy Insulinemia increased during pregnancy with reduced glycemia, characterizing hormonal resistance. Leptin and prolactin were also increased during pregnancy, being the highest increase in observed in HP rats. Protein restriction in pregnancy modified maternal metabolism, altering lipid synthesis in the liver and hormonal profile and decreasing the placenta and fetus masses.
Descritores: Dieta com Restrição de Proteínas/efeitos adversos
Fenômenos Fisiológicos da Nutrição Materna/fisiologia
-Análise de Variância
Tecido Adiposo/metabolismo
Feto/metabolismo
Gônadas/metabolismo
Hormônios/biossíntese
Lipídeos/biossíntese
Glicogênio Hepático/biossíntese
Fígado/química
Fígado/enzimologia
Modelos Animais
Malato Desidrogenase/biossíntese
Glândulas Mamárias Animais/metabolismo
Placenta/metabolismo
Ratos Wistar
Limites: Animais
Feminino
Gravidez
Ratos
Responsável: BR1.1 - BIREME


  7 / 21 LILACS  
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Id: lil-484608
Autor: Aquino-Silva, Maria Regina de; Schwantes, Maria Luiza Barcellos; Munin, Flavia Simone; Schwantes, Arno Rudi; Santos, Silvana Pereira dos.
Título: Soluble malate dehydrogenase of Geophagus brasiliensis (Cichlidae, Perciformes): isolated isoforms and kinetics properties
Fonte: Genet. mol. biol;31(1,suppl):337-342, 2008. ilus, graf.
Idioma: en.
Resumo: Kinetic properties and thermal stabilities of Geophagus brasiliensis skeletal muscle unfractionated malate dehydrogenase (MDH, EC 1.1.1.37) and its isolated isoforms were analyzed to examine a possible sMDH-B* locus duplication in a fixation process influenced by genetic drift. Two optimal pHs were detected: 7.5 for AB1 unfractionated muscle phenotype and its B1 isoform, and 8.0 for AB1B2 unfractionated muscle phenotype, A and B2 isoforms. While G. brasiliensis A isoform could be characterized as thermostable, the duplicated B isoform cannot be assumed as thermolabile. Km values for isolated B2 isoforms were 1.6 times lower than for B1. A duplication event in progress best explains the electrophoretic six-band pattern detected in G. brasiliensis, which would be caused by genetic drift.
Descritores: Malato Desidrogenase
Perciformes/genética
-Duplicação Gênica
Peixes/genética
Limites: Animais
Responsável: BR26.1 - Biblioteca Central


  8 / 21 LILACS  
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Id: lil-343407
Autor: Aquino-Silva, M. R; Schwantes, M. L. B; Schwantes, A. R.
Título: Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes)
Fonte: Braz. j. biol;63(1):7-15, Feb. 2003. ilus, graf.
Idioma: en.
Resumo: Kinetic properties and thermal stabilities of Hoplias malabaricus liver and skeletal muscle unfractionated malate dehydrogenase (MDH, EC 1.1.1.37) and its isolated isoforms were analyzed to further study the possible sMDH-A* locus duplication evolved from a recent tandem duplication. Both A (A1 and A2) and B isoforms had similar optima pH (7.5-8.0). While Hoplias A isoform could not be characterized as thermostable, B could as thermolabile. A isoforms differed from B isoform in having higher Km values for oxaloacetate. The possibly duplicated A2 isoform showed higher substrate affinity than the A1. Hoplias duplicated A isoforms may influence the direction of carbon flow between glycolisis and gluconeogenesis
Descritores: Peixes
Duplicação Gênica
Isoenzimas
Malato Desidrogenase
-Eletroforese em Gel de Amido
Concentração de Íons de Hidrogênio
Cinética
Malato Desidrogenase
Temperatura
Limites: Animais
Responsável: BR1.1 - BIREME


  9 / 21 LILACS  
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Id: lil-308284
Autor: Panepucci, R. A; Panepucci, L; Fernandes, M. N; Sanches, J. R; Rantin, F. T.
Título: The effect of hypoxia and recuperation on carbohydrate metabolism in pacu (Piaractus mesotamicus)
Fonte: Braz. j. biol;61(4):547-554, Nov. 2001. graf.
Idioma: en.
Resumo: A study of the hematological parameters, glycogen, glucose, and lactate, and the activity of malate and lactate dehydrogenases was carried out in blood and tissues of fishes submitted to two, four, and six hours of hypoxia and recuperation. Only after 4 h of hypoxia was there a drop in liver glucose. After 6 h, a drop in lactate and a rise in glucose in practically all tissues signaled a recuperation of the metabolism, probably due to ASR (aerial surface respiration). Lactate formed during hypoxia was canalized to heart and brain for oxidation and used for neoglucogenesis. There were no changes in hematological parameters nore in the activity of malate and lactate dehydrogenases during normoxia and hypoxia, which suggest that these adaptive mechanisms may not be involved during hypoxia. Glycogen concentrations did not show variation during hypoxia either
Descritores: Oxirredutases do Álcool
Carboidratos
Peixes
Hipóxia
Lactatos
-Glucose
Glicogênio
Hipóxia
L-Lactato Desidrogenase
Malato Desidrogenase
Fatores de Tempo
Limites: Animais
Responsável: BR1.1 - BIREME


  10 / 21 LILACS  
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Id: lil-262068
Autor: Penepucci, L; Fernandes, M. N; Sanches, J. R; Rantin, F. T.
Título: Changes in lactate dehydrogenase and malate dehydrogenase activities during hypoxia and after temperature acclimation in the armored fish, Rhinelepis strigosa (Siluriformes, Loricariidae)
Fonte: Rev. bras. biol;60(2):353-60, May 2000. tab, graf.
Idioma: en.
Resumo: Lactate (LDH) and malate dehydrogenase (MDH) of white skeletal muscle of fishes acclimated to 20, 25 and 30 degrees Celsius and thereafter submitted to hypoxia were studied in different sbstrate concentrations. Significant differences for LDH and MDH of white muscle enzyme activities are described here for the first time in Rhinelepis strigosa of fishes acclimated to 20 degrees Celsius and submitted to hypoxia for six hours. LDH presented a significant decrease in enzyme affinity for pyruvate in acute hypoxia, for fishes acclimated to 20 degrees Celsius and an increase for fishes acclimated to 30 degrees Celsius.
Descritores: Aclimatação
Peixes/metabolismo
Hipóxia/metabolismo
L-Lactato Desidrogenase/metabolismo
Malato Desidrogenase/metabolismo
Músculo Esquelético/enzimologia
Temperatura
Limites: Animais
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME



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