Sabiia Seb
PortuguêsEspañolEnglish
Embrapa
        Busca avançada

Botão Atualizar


Botão Atualizar

Ordenar por: RelevânciaAutorTítuloAnoImprime registros no formato resumido
Registros recuperados: 3
Primeira ... 1 ... Última
Imagem não selecionada

Imprime registro no formato completo
Age-related changes in glucose utilization and fatty acid oxidation in a muscle-specific manner during rabbit growth Inra
Gondret, F.; Damon, M.; Jadhao, S.B.; Houdebine, L.M.; Herpin, P.; Hocquette, J.F..
The optimal utilization of energy substrates in muscle fibers is of primary importance for muscle contraction and whole body physiology. This study aimed to investigate the age-related changes in some indicators of glucose catabolism and fatty acid oxidation in muscles of growing rabbits. Longissimus lumborum (fast-twitch, LL) and semimembranosus proprius (slow-twitch, SMP) muscles were collected at 10 or 20 weeks of age (n = 6 per age). Glucose transporter GLUT4 content was investigated by immunoblot assay. Activity levels of five enzymes were measured: lactate dehydrogenase (LDH) and phosphofructokinase (PFK) for glycolysis; citrate synthase (CS), isocitrate dehydrogenase (ICDH) and -3-hydroxyacyl-coenzyme A dehydrogenase (HAD) for oxidation....
Tipo: Journal Article Palavras-chave: CITRATE SYNTHASE; CONTRACTION MUSCULAIRE; CROISSANCE; GLUT4; L-3-HYDROXYACIL-COENZYME A DESHYDROGENASE; LACTATE DESHYDROGENASE; METABOLISME DU GLUCOSE; METABOLISME MUSCULAIRE; PHOSPHOFRUCTOKINASE METABOLIC TYPE; BETA-OXIDATION; GLUCOSE TRANSPORTER; PEROXISOMES; SKELETAL MUSCLE.
Ano: 2004 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=00111709&uri=/notices/prodinra1/2010/12/
Imagem não selecionada

Imprime registro no formato completo
Lactate dehydrogenase as a marker of Plasmodium infection in malaria vector Anopheles IRD
Riandey, Marie-France; Sannier, Christiane; Peltre, G.; Monteny, Nicole; Cavaleyra, Mireille.
Lactate dehydrogenase (Ldh) electrophoresis showed the presence of #Plasmodium yoelii yoelii$ in #Anopheles stephensi$ and #An. gambiae$. The Ldh appeared as an additional band (pLdh) whose activity was more intense with 3-acetyl pyridine adenine dinucleotide as coenzyme than with beta nicotinamide adenine dinucleotide. Several allelic forms occurred both in the vector and the host. The isoelectric point of Ldh, similar in the vector and host, differed from those of Ldh from mosquito and mouse. The presence of pLdh was detected from the 2nd to the 28th day of infection. The pLdh appeared to be proportional to the number of sporozoites present in infected salivary glands. However, pLdh was not found in salivary glands or midguts, but it was detected in the...
Tipo: Text Palavras-chave: ENTOMOLOGIE MEDICALE; PALUDISME; EPIDEMIOLOGIE; INFECTION; ENZYME; DOSAGE; LACTATE DESHYDROGENASE; ELECTROPHORESE.
Ano: 1996 URL: http://www.documentation.ird.fr/hor/fdi:010006783
Imagem não selecionada

Imprime registro no formato completo
Nicotinic acid controls lactate production by K1-LDH: a Saccharomyces cerevisiae strain expressing a bacterial LDH gene Inra
Colombié, S.; Sablayrolles, J.M..
Industrial applications for lactate, such as the production of chemicals, has led to interest in producing this organic acid by metabolically engineered a yeast such as Saccharomyces cerevisiae, which is more acid tolerant than lactic acid bacteria. This paper deals with lactate production by S. cerevisiae K1-LDH, in which the Lactobacillus plantarum lactate dehydrogenase (LDH) gene is integrated into the genome of the wine yeast strain K1. We show that a vitamin, nicotinic acid (NiA), was the limiting factor for lactate production during fermentation with the K1-LDH strain. Increasing the NiA concentration in batch conditions or in the medium used to feed chemostats affected the lactate yield. Moreover, the addition of pulses of NiA or the exponential...
Tipo: Journal Article Palavras-chave: ACIDE NICOTINIQUE; L-LACTATE; LACTATE DESHYDROGENASE; SACCHAROMYCES CEREVISIAE; OENOLOGIE; EXPRESSION DES GENES NICOTINIC ACID; L-LACTATE; ALCOHOLIC FERMENTATION; LACTATE DEHYDROGENASE; SACCHAROMYCES CEREVISIAE.
Ano: 2004 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0400025097104741&uri=/notices/prodinra1/2010/11/
Registros recuperados: 3
Primeira ... 1 ... Última
 

Empresa Brasileira de Pesquisa Agropecuária - Embrapa
Todos os direitos reservados, conforme Lei n° 9.610
Política de Privacidade
Área restrita

Embrapa
Parque Estação Biológica - PqEB s/n°
Brasília, DF - Brasil - CEP 70770-901
Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco

Valid HTML 4.01 Transitional