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Texto completo SciELO Saúde Pública
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Id: lil-733306
Autor: Rivera-Ávila, Roberto Carlos.
Título: Fiebre chikungunya en México: caso confirmado y apuntes para la respuesta epidemiológica / Chikungunya fever in Mexico: confirmed case and notes on the epidemiologic response
Fonte: Salud pública Méx;56(4):402-404, jul.-ago. 2014. tab.
Idioma: es.
Resumo: La fiebre chikungunya (CHIK) es una enfermedad viral transmitida al ser humano por el mismo vector del dengue, el mosquito Aedes. Además de fiebre y fuertes dolores articulares, produce otros síntomas como mialgias, cefalea, náuseas, cansancio y exantema. No tiene tratamiento específico; el manejo terapéutico de los pacientes se enfoca en el alivio de los síntomas. Históricamente se han reportado brotes de grandes proporciones; incluso desde 2010 se llegó a considerar como una potencial epidemia emergente. En 2013 se introdujo a las islas del Caribe y recientemente se ha reportado en el continente americano. En este trabajo se describe el primer caso confirmado de chikungunya en México, en el municipio de Tlajomulco de Zúñiga, Jalisco, en mayo de 2014, importado de la isla Antigua y Barbuda, en el Caribe, por una mujer de 39 años de edad.

Chikungunya fever (CHIK) is a viral disease transmitted to human beings by the same vector as dengue -the Aedes mosquito. Besides fever and severe pain in the joints, it produces other symptoms such as myalgias, headache, nausea, fatigue and exanthema. There is no specific treatment for it; the therapeutic management of patients focuses on symptom relief. Historically, outbreaks of large proportions have been reported; even since 2010 it was considered to be a potential emerging epidemic. In 2013 it was introduced into the islands of the Caribbean, and it has recently been reported in the American continent. This paper describes the first confirmed case of chikungunya in Mexico -in the municipality of Tlajomulco de Zúñiga, Jalisco, in May, 2014-, which was imported from the Caribbean island of Antigua and Barbuda by a 39 year-old woman.
Descritores: Antídotos/farmacologia
Temperatura Alta
Imidazóis/toxicidade
Carne
Mitocôndrias/metabolismo
Mutagênicos/toxicidade
Consumo de Oxigênio/efeitos dos fármacos
Ubiquinona/farmacologia
-Antídotos/administração & dosagem
Culinária
Dieta
Complexo II de Transporte de Elétrons
Complexo III da Cadeia de Transporte de Elétrons/metabolismo
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Transporte de Elétrons/efeitos dos fármacos
Alimentos Fortificados
Mitocôndrias Cardíacas/efeitos dos fármacos
Mitocôndrias Cardíacas/metabolismo
Mitocôndrias Hepáticas/efeitos dos fármacos
Mitocôndrias Hepáticas/metabolismo
Mitocôndrias Musculares/efeitos dos fármacos
Mitocôndrias Musculares/metabolismo
Complexos Multienzimáticos/metabolismo
NAD(P)H Desidrogenase (Quinona)/metabolismo
Oxirredutases/metabolismo
Ratos Wistar
Succinato Desidrogenase/metabolismo
Ubiquinona/administração & dosagem
Limites: Animais
Bovinos
Masculino
Ratos
Responsável: BR1.1 - BIREME


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Id: lil-698755
Autor: Osorio, Edison; Aguilera, Carolina; Naranjo, Nelson; Marín, Marcel; Muskus, Carlos.
Título: Biochemical characterization of the bifunctional enzyme dihydrofolate reductase-thymidylate synthase from Leishmania ( Viannia ) and its evaluation as a drug target / Caracterización bioquímica de la enzima bifuncional dihidrofolato reductasa-timidilato sintasa de Leishmania ( Viannia ) y su evaluación como blanco molecular
Fonte: Biomédica (Bogotá);33(3):393-401, set. 2013. ilus, graf, tab.
Idioma: en.
Resumo: Introduction. Dihydrofolate reductase (DHFR) has been used successfully as a drug target in the area of anti-bacterial, anti-cancer and anti-malarial therapy. Although this bifunctional enzyme is also a potential drug target for treatment of leishmaniasis, there have been no reports on its efficacy against Leishmania ( Viannia ) species . Materials and methods. The gene encoding the bifunctional DHFR and thymidylate synthase (TS) of Le. (V.) braziliensis was isolated and expressed in E. coli. The enzyme was purified and characterized. The inhibitory effects of antifolates and four aporphine alkaloids on its activity were evaluated. Results. The full-length gene consists of a 1560-bp open reading frame encoding a 58 kDa translated peptide containing DHFR and TS domains linked together in a single polypeptide chain. The recombinant DHFR-TS enzyme revealed K m and V max values of 55.35 ± 4.02 µ M (mean ± SE) and 0.02 ± 5.34 x 10 -4 µ M/min respectively for dihydrofolic acid (H 2 F). The Le. braziliensis rDHFR-TS have Ki values for antimicrobial antifolates in the µM range. Methotrexate (MTX) was a more-potent inhibitor of enzymatic activity ( Ki = 22.0 µM) than trimethoprim ( Ki = 33 µM) and pyrimethamine ( Ki = 68 µM). These Ki values are significantly lower than those obtained for the aporphine alkaloids. Conclusion. The results of the study show the inhibitory effect of antifolate drugs on enzymatic activity, indicating that Le. braziliensis rDHFR-TS could be a model to studying antifolate compounds as potential antiprotozoal drugs.

Introducción. La dihidrofolato reductasa (DHFR) se ha utilizado como blanco molecular en tratamientos antibacterianos, anticancerígenos y antipalúdicos. También, actúa como blanco molecular en Leishmania ; sin embargo, no existen reportes de la enzima bifuncional en especies de Leishmania ( Viannia ). Materiales y métodos. Se ha aislado y expresado en Escherichia coli el gen que codifica para la enzima bifuncional DHFR y la timidilato-sintasa (TS) de Leishmania braziliensis . La enzima recombinante se purificó y caracterizó, y se evaluó el efecto inhibitorio de algunos antifolatos, así como de cuatro alcaloides aporfínicos. Resultados. El gen se compone de aproximadamente 1.560 pb y codifica un péptido de 58 kDa que contiene los dominios DHFR y TS ligados en una sola cadena polipeptídica. La enzima recombinante DHFR-TS, utilizando el dihidrofolato (H2F) como sustrato, presentó valores de K m y V max de 55,35 ± 4,02 (media ± el error estándar de la media) y de 0,02 ± 5,34 x 10 -4 , respectivamente. La enzima rDHFR-TS de L. braziliensis presentó valores de Ki para los antifolatos en el rango de micras. El metotrexato fue el inhibidor más potente de la actividad enzimática ( Ki =22,0 mM) en comparación del trimetoprim ( Ki =33 mM) y la pirimetamina ( Ki =68 mM). Estos valores de Ki son significativamente más bajos en comparación con los obtenidos para los alcaloides aporfínicos. Conclusión. Los resultados muestran el efecto inhibitorio de los antifolatos sobre la actividad enzimática, lo cual indica que la rDHFR-TS de L. braziliensis podría ser un modelo para estudiar moléculas antiprotozoarias potenciales.
Descritores: Antagonistas do Ácido Fólico/farmacologia
Leishmania/enzimologia
Complexos Multienzimáticos/antagonistas & inibidores
Complexos Multienzimáticos/química
Tetra-Hidrofolato Desidrogenase/química
Timidilato Sintase/antagonistas & inibidores
Timidilato Sintase/química
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: CO332 - Facultad de Medicina


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Texto completo SciELO Cuba
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Id: lil-648605
Autor: Hernández Betancourt, Oscar; Fernández Torres, Sandra; Vázquez Reyes, Nayadis; Leiva Quesada, Lydice; Falcón Almeida, Yadira; Torres Romo, Ubaldo.
Título: Estabilidad de un suero control multienzimático utilizado como material de referencia en los laboratorios clínicos / Stability of a multienzyme control serum used as reference material in clinical laboratories
Fonte: Rev. cuba. invest. bioméd;31(2):0-0, abr.-jun. 2012.
Idioma: es.
Resumo: Una de las vías fundamentales para garantizar la calidad de los ensayos realizados en los laboratorios clínicos es mediante el uso de materiales de referencia. Una problemática a la que nos enfrentamos es la escasez de estos productos en el mercado nacional dado su alto costo. Objetivo: evaluar la estabilidad de un suero bovino adulto enriquecido con las enzimas alanina aminotransferasa (ALAT/TGP), aspartato aminotransferasa (ASAT/TGP), fosfatasa alcalina (FA) y amilasa. Métodos: se evaluó la estabilidad a tiempo real de la matriz enriquecida con las diferentes enzimas durante 12 meses a 2 temperaturas (refrigeración y congelación). Se evaluó el efecto del glicerol sobre la actividad enzimática de los extractos, así como el efecto de los preservantes propilenglicol y etilenglicol en la estabilidad de las enzimas. Resultados: los extractos enzimáticos obtenidos comenzaron a perder la actividad biológica a partir de los 15 días, independientemente de la temperatura de almacenamiento y de la presencia o no de glicerol. Los resultados del ensayo a tiempo real realizados a la matriz enriquecida, mostraron que la estabilidad varió con el tiempo y con el tipo de enzima, independientemente del preservante ensayado, disminuyendo por debajo de los límites aceptables de actividad enzimática luego de 3 meses de almacenamiento del producto a 4 ºC. Conclusiones: se logró un material de referencia multienzimático estable por un período de 3 meses

A fundamental method to assure the quality of clinical laboratory tests is the use of reference materials. A problem we are faced with is the scarcity of these products in the domestic market, due their high cost. Objective: Evaluate the stability of an adult bovine serum enriched with the enzymes alanine aminotransferase (ALT, GPT), aspartate aminotransferase (AST, GPT), alkaline phosphatase (AP) and amylase. Methods: This enzyme-enriched matrix underwent real-time stability assessment during 12 months at two temperatures (refrigerated and frozen). An evaluation was made of the effect of glycerol on the enzymatic activity of extracts, as well as the effect of the preservatives propylene glycol and ethylene glycol on enzymatic stability. Results: The enzyme extracts obtained began to lose their biological activity at 15 days, irrespective of the storage temperature and the presence or absence of glycerol. The real time assessment of the enriched matrix showed that stability varied with time and enzyme type, irrespective of the preservative tested, and fell below acceptable limits of enzymatic activity after three months of storage at 4 ºC. Conclusions: A multienzyme reference material was obtained which was stable for a period of 3 months
Descritores: Complexos Multienzimáticos/síntese química
Estabilidade Enzimática
Reagentes de Laboratório
-Padrões de Referência
Limites: Animais
Coelhos
Responsável: CU1.1 - Biblioteca Médica Nacional


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Texto completo SciELO Brasil
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Id: lil-424750
Autor: Pacheco, Flávia Teresa Hansen; Silva-Stenico, Maria Estela; Etchegaray, Augusto; Gomes, José Elias; Carrilho, Emanuel; Tsai, Siu Mui.
Título: Specific amplification of iron receptor genes in Xylella fastidiosa strains from different hosts
Fonte: Genet. mol. biol;29(1):137-141, 2006. tab.
Idioma: en.
Projeto: Fundação de Amparo à Pesquisa do Estado de São Paulo.
Resumo: Bacterial production of siderophores may involve specific genes related to nonribosomal peptide and polyketide biosynthesis, which have not been fully identified in the genome of Xylella fastidiosa strain 9a5c. However, a search for siderophore-related genes in strain 9a5c indicated five membrane receptors, including siderophore, ferrichrome-iron and hemin receptors. All these biomolecules are thought to be associated with iron transport and utilization. Eighty isolates obtained from citrus orchards containing trees that developed citrus variegated chlorosis (CVC) were screened for siderophore production. The results demonstrated that only 10 of the isolates did not produce siderophores. Additional strains obtained from coffee, almond, mulberry, elm, ragweed, periwinkle and grape also infected by X. fastidiosa were also shown by the chromeazurol bioassay to produce siderophores. In order to correlate siderophore production with the presence of siderophore-related genes, a polymerase chain reaction (PCR) was developed using specific primers for the catechol-type ferric enterobactin receptor (pfeA) and the hydroxamate-type ferrisiderophore receptor (fiuA) genes of strain 9a5c. The PCR results confirmed our hypothesis by demonstrating that amplification products were detected in all strains except for those isolates that did not produce siderophores.
Descritores: Complexos Multienzimáticos
Biossíntese de Peptídeos Independentes de Ácido Nucleico
Xylella/genética
-Doenças das Plantas/microbiologia
Enterobactina
Bactérias Gram-Negativas
Reação em Cadeia da Polimerase
Limites: Animais
Responsável: BR26.1 - Biblioteca Central


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Id: lil-417595
Autor: Miyoshi, A; Rochat, T; Gratadoux, J. J; Le Loir, Y; Oliveira, S. C; Langella, P; Azevedo, V.
Título: Oxidative stress in Lactococcus lactis
Fonte: Genet. mol. res. (Online);2(4):348-359, Dec. 2003.
Idioma: en.
Resumo: Lactococcus lactis, the most extensively characterized lactic acid bacterium, is a mesophilic- and microaerophilic-fermenting microorganism widely used for the production of fermented food products. During industrial processes, L. lactis is often exposed to multiple environmental stresses (low and high temperature, low pH, high osmotic pressure, nutrient starvation and oxidation) that can cause loss or reduction of bacterial viability, reproducibility, as well as organoleptic and/or fermentative qualities. Among these stress factors, oxidation can be considered one of the most deleterious to the cell, causing cellular damage at both molecular and metabolic levels. During the last two decades, considerable efforts have been made to improve our knowledge of oxidative stress in L. lactis. Many genes involved with both oxidative stress resistance and control mechanisms have been identified; functionally they seem to overlap. The finding of new genes, and a better understanding of the molecular mechanisms of stress resistance in L. lactis and other lactic acid bacterium, will lead to the construction and isolation of stress-resistant strains. Such strains could be exploited for both traditional and probiotic uses
Descritores: Estresse Oxidativo/fisiologia
Lactococcus lactis/metabolismo
-Complexos Multienzimáticos/metabolismo
Estresse Oxidativo/genética
Genes Bacterianos/genética
Lactococcus lactis/genética
NADH NADPH Oxirredutases/metabolismo
Peroxidases/metabolismo
Recombinases Rec A/metabolismo
Sobrevivência Celular/genética
Superóxido Dismutase/metabolismo
Tipo de Publ: Research Support, U.S. Gov't, Non-P.H.S.
Responsável: BR1.1 - BIREME


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Id: lil-417582
Autor: Antônio, R. V; Creczynski-Pasa, T. B.
Título: Genetic analysis of violacein biosynthesis by Chromobacterium violaceum
Fonte: Genet. mol. res. (Online);3(1):85-91, Mar. 2004.
Idioma: en.
Resumo: Chromobacterium violaceum presents a distinctive phenotypic characteristic, the production of a deep violet pigment named violacein. Although the physiological function of this pigment is not well understood, the sequencing of the genome of this bacterium has given some insight into the mechanisms and control of violacein production. It was found that erythrose-4-phosphate (E4P), a precursor to aromatic amino acid biosynthesis, is produced by the non-oxidative portion of the hexose monophosphate pathway, since it lacks 6-phosphogluconate dehydrogenase. All genes leading from E4P plus phosphoenolpyruvate to tryptophan are present in the genome. Nevertheless, these genes are not organized in an operon, as in E. coli, indicating that other mechanisms are involved in expression. The sequencing data also indicated the presence and organization of an operon for violacein biosynthesis. Three of the four gene products of this operon presented similarity with nucleotide-dependent monooxygenases and one with a limiting enzyme polyketide synthase. As previously suggested, genes encoding proteins involved in quorum sensing control by N-hexanoyl-homoserine-lactone, an autoinducer signal molecule, are present in the bacterial genome. These data should help guide strategies to increase violacein biosynthesis, a potentially useful molecule
Descritores: Chromobacterium/genética
Indóis/metabolismo
-Chromobacterium/metabolismo
Complexos Multienzimáticos/biossíntese
Complexos Multienzimáticos/genética
Fosfatos Açúcares/genética
Fosfatos Açúcares/metabolismo
Hidrolases de Éster Carboxílico/biossíntese
Hidrolases de Éster Carboxílico/genética
Indóis/química
Triptofano/biossíntese
Triptofano/genética
Tipo de Publ: Research Support, U.S. Gov't, Non-P.H.S.
Responsável: BR1.1 - BIREME


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Id: lil-387948
Autor: Drider, Djamel; Bekal, Sadjia; Prevost, Herve.
Título: Genetic organization and expression of citrate permease in lactic acid bacteria
Fonte: Genet. mol. res. (Online);3(2):273-281, jun. 2004.
Idioma: en.
Resumo: Citrate is present in many natural substrates, such as milk, vegetables and fruits, and its metabolism by lactic acid bacteria (LAB) plays an important role in food fermentation. The industrial importance of LAB stems mainly from their ability to convert carbohydrates into lactic acid and, in some species, like Lactococcus lactis and Leuconostoc mesenteroides, to produce C4 flavor compounds (diacetyl, acetoin) through citrate metabolism. Three types of genetic organization and gene locations, involving citrate metabolism, have been found in LAB. Citrate uptake is mediated by a citrate permease, which leads to a membrane potential upon electrogenic exchange of divalent citrate and monovalent lactate. The internal citrate is cleaved into acetate and oxaloacetate by a citrate lyase, and oxaloacetate is decarboxylated into pyruvate by an oxaloacetate decarboxylase, yielding a pH gradient through the consumption of scalar protons.
Descritores: Proteínas de Bactérias
Proteínas de Transporte
Ácido Láctico
Lactococcus
Complexos Multienzimáticos
Oxo-Ácido-Liases
-Proteínas de Bactérias
Sequência de Bases
Proteínas de Transporte
Diacetil
DNA Bacteriano
Lactococcus
Dados de Sequência Molecular
Complexos Multienzimáticos
Fases de Leitura Aberta
Oxo-Ácido-Liases
Responsável: BR1.1 - BIREME


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Id: lil-245926
Autor: Burgos, Carlos; Civallero, Gabriel E; Kremer, Raquel D. de; Geres de Burgo, Nelia M; Blanco, Antonio.
Título: Enzymatic method for branched chain alpha-ketoacid determination: application to rapid analysis of urine and plasma samples from maple syrup urine disease patients
Fonte: Acta physiol. pharmacol. ther. latinoam;49(2):109-7, 1999. tab.
Idioma: en.
Resumo: A new method for the determination of branched-chain alpha-ketoacid concentration using lactate dehydrogenase (E C 1.1.1.27) isozyme C4 (LDH) C4) from mouse testes is proposed. The assay is performed on urine and plasma without previous treatment. Alpha-ketoglutarate and pyruvate are determined on the same sample using glutamate dehydrogenase (GDH,EC 1.4.1.2) and lactate dehydrogenase isozyme A4 (LDH5) respectively and subtracted from the total alpha-ketoacid concentration obtained with LDH C4. This value corresponds to the branched chain alpha-ketoacid. Results were linear within the concentration range 8 to 170 mumoles/L. Detection limit was 8 mumoles/L. Analytical recovery was higher than 91 per cent. For microplate assays, recoveries were higher than 84 per cent and the detection limit was 20 mumoles/L. Determinations performed with GDH, LDH A4 and LDH C4 allow differentiation of E3 deficiency from other clinical phenotypes of maple syrup urine disease. The method is simple and fast, and adaptation to microplates would allow screening of newborns.
Descritores: Ensaios Enzimáticos Clínicos
L-Lactato Desidrogenase/sangue
L-Lactato Desidrogenase/urina
Doença da Urina de Xarope de Bordo/diagnóstico
Complexos Multienzimáticos/sangue
Complexos Multienzimáticos/urina
-Cromatografia Gasosa
Glutamato Desidrogenase/análise
Doença da Urina de Xarope de Bordo/genética
Desidrogenase do Álcool de Açúcar/análise
Testículo/enzimologia
Limites: Adulto
Humanos
Feminino
Criança
Pré-Escolar
Adolescente
Animais
Ratos
Responsável: BR1.1 - BIREME


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Val, Adalberto Luis
Id: lil-209331
Autor: Val, Adalberto Luis.
Título: Carbonic anhydrase: a multigene-multifunctional enzyme
Fonte: An. acad. bras. ciênc;69(4):565-73, 1997.
Idioma: en.
Resumo: Carbonic anhydrase is a zinc metalloenzyme that catalyzes the simple interconversion between carbon dioxide (CO2) and bicarbonate (HCO3). Seven genes encode the CA isozymes in vertebrates. They are single chain peptides termed CAI-VII. One CA isozyme is present in teleost fish. Three isozymes clearly appear together in birds. All seven types appear in mammals. Despite the great similarity among these isozymes, they present strong differences with respect to their kinetic properties. Many physiological and biochemical processes are related to the activity of CA isozymes.
Descritores: Evolução Biológica
Anidrases Carbônicas/genética
Regulação Enzimológica da Expressão Gênica
Complexos Multienzimáticos/genética
Plantas/enzimologia
-Inibidores da Anidrase Carbônica
Anidrases Carbônicas/metabolismo
Cinética
Limites: Animais
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


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Id: lil-30097
Autor: Ureta, Tito; Radojkovié, Jasna.
Título: Search for compartments of glucose metabolism in the microinjected frog oocyte
Fonte: Arch. biol. med. exp;18(3/4):253-9, dic. 1985. tab.
Idioma: en.
Conferência: Apresentado em: Annual Meeting of the Sociedad de Bioquímica de Chile, 8, Cartagena, Aug. 6-8 1984.
Descritores: Compartimento Celular
Glucose/metabolismo
Complexos Multienzimáticos/metabolismo
Oócitos/metabolismo
-Anuros
Glicogênio/biossíntese
Via de Pentose Fosfato
Limites: Animais
Responsável: BR1.1 - BIREME



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