Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 3 de 3
Filtrar
Mais filtros










Base de dados
Intervalo de ano de publicação
1.
Biochem Biophys Res Commun ; 423(4): 781-4, 2012 Jul 13.
Artigo em Inglês | MEDLINE | ID: mdl-22713453

RESUMO

Three coenzyme A (CoA) molecular species, i.e., acetyl-CoA, malonyl-CoA, and nonesterified CoA (CoASH), in 13 types of fasted rat tissue were analyzed. A relatively larger pool size of total CoA, consisting of acetyl-CoA, malonyl-CoA, and CoASH, was observed in the medulla oblongata, liver, heart, and brown adipose tissue. Focusing on changes in the CoA pool size in response to the nutrient composition of the diet given, total CoA pools in rats continuously fed a high-fat diet for 4 weeks were significantly higher in the hypothalamus, cerebellum, and kidney, and significantly lower in the liver and skeletal muscle than those of rats fed a high-carbohydrate or high-protein diet. In particular, reductions in the liver were remarkable and were caused by decreased CoASH levels. Consequently, the total CoA pool size was reduced by approximately one-fifth of the hepatic contents of rats fed the other diets. In the hypothalamus, which monitors energy balance, all three CoA molecular species measured were at higher levels when rats were fed the high-fat diet. Thus, it was of interest that feeding rats a high-fat diet affected the behaviors of CoA pools in the hypothalamus, liver, and skeletal muscle, suggesting a significant relationship between CoA pools, especially malonyl-CoA and/or CoASH pools, and lipid metabolism in vivo.


Assuntos
Acetilcoenzima A/metabolismo , Coenzima A/metabolismo , Dieta Hiperlipídica/efeitos adversos , Malonil Coenzima A/metabolismo , Animais , Peso Corporal , Ingestão de Energia , Hipotálamo/enzimologia , Metabolismo dos Lipídeos , Fígado/enzimologia , Masculino , Músculo Esquelético/enzimologia , Obesidade/etiologia , Especificidade de Órgãos , Ratos , Ratos Wistar , Distribuição Tecidual , Aumento de Peso
2.
Biochem Biophys Res Commun ; 402(1): 158-62, 2010 Nov 05.
Artigo em Inglês | MEDLINE | ID: mdl-20933504

RESUMO

Levels of three coenzyme A (CoA) molecular species, i.e., nonesterified CoA (CoASH), acetyl-CoA, and malonyl-CoA, in fasted and fed rat tissues were analyzed by the acyl-CoA cycling method which makes detection possible at the pmol level. Malonyl-CoA in brain tissues readily increased with feeding, and inversely, acetyl-CoA decreased. This phenomenon occurred in the cerebral cortex, hippocampus, cerebellum, and medulla oblongata, as well as in the hypothalamus which controls energy balance by monitoring malonyl-CoA. In the non-brain tissues, the sizes of the acetyl-CoA, malonyl-CoA, and CoASH pools depended on the tissues. The total CoA pools consisting of the above three CoA species in the liver, heart, and brown adipose tissue were larger and those of the perirenal, epididymal, and ovarian adipose tissues were much smaller, compared with those of other tissues including brain tissues. In addition, the response of each CoA pool to feeding was not uniform, suggesting that the tissue-specific metabolism individually functions in the non-brain tissues. Thus, a comprehensive analysis of thirteen types of rat tissue revealed that CoA pools have different sizes and showed a different response to fasting and feeding depending on the tissue.


Assuntos
Acetilcoenzima A/metabolismo , Coenzima A/metabolismo , Ingestão de Alimentos , Jejum/metabolismo , Malonil Coenzima A/metabolismo , Acetilcoenzima A/análise , Animais , Encéfalo/enzimologia , Coenzima A/análise , Feminino , Masculino , Malonil Coenzima A/análise , Ratos , Ratos Wistar , Distribuição Tecidual
3.
Biosci Biotechnol Biochem ; 71(10): 2577-80, 2007 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-17928689

RESUMO

The cellulose-binding proteins, CBPA and CBPB, of rumen cellulolytic bacterium Eubacterium cellulosolvens 5 were biochemically characterized, and their properties were compared. Recombinant CBPA and CBPB were a typical 1,4-beta-endoglucanase. Both proteins bound to insoluble polysaccharides such as Avicel cellulose, acid swollen cellulose, lichenan, chitin, and oat spelt xylan. On the other hand, only recombinant CBPB bound to agarose and starch.


Assuntos
Proteínas de Bactérias/química , Proteínas de Bactérias/metabolismo , Celulose/metabolismo , Eubacterium/química , Rúmen/microbiologia , Animais , Proteínas de Bactérias/genética , Celobiose/biossíntese , Celulose 1,4-beta-Celobiosidase/metabolismo , Cromatografia em Camada Fina , Eletroforese em Gel de Poliacrilamida , Escherichia coli/genética , Glucose/biossíntese , Concentração de Íons de Hidrogênio , Hidrólise , Peso Molecular , Plasmídeos , Proteínas Recombinantes/química , Proteínas Recombinantes/isolamento & purificação , Proteínas Recombinantes/metabolismo , Especificidade por Substrato , Temperatura
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...