Base de dados : MedCarib
Pesquisa : D01.268.150.075 [Categoria DeCS]
Referências encontradas : 12 [refinar]
Mostrando: 1 .. 10   no formato [Longo]

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  1 / 12 MedCarib  
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Fotocópia
Id: 15855
Autor: Stephen, Joan M. L; Waterlow, John C.
Título: Use of carbon-14-labelled arginine to measure the catabolic rate of serum and liver proteins and the extent of amino-acid recycling
Fonte: Nature;211(52):978-80, Aug. 27, 1966.
Idioma: En.
Responsável: JM3.1 - Médical Library
JM9.1; Q1.N38


  2 / 12 MedCarib  
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Fotocópia
Id: 15824
Autor: Waterlow, John C; Stephen, Joan M. L.
Título: The measurement of total lysine turnover in the rat by intravenous infusion of L-[U-14C] lysine
Fonte: Clin Sci;33(3):489-506, Dec. 1967.
Idioma: En.
Resumo: Rats were infused intravenously for periods up to 7 hr with L-[U-14C]lysine. After about 4 hr the specific activity of free lysine in the blood reached a plateau. From the value of the plateau specific activity it is possible to calculate the total lysine flux into or out of the blood stream. In normal rats the flux is equivalent to a total protein turnover of 25-30 g kg-1 day-1. In male, but not in female rats the total flux decreased significantly with increasing body weight or age. Six weeks of protein depletion caused a decrease of 30 percent in the flux. Alloxan diabetes in a small number of rats caused no significant change. After the first ½ hr of the infusion the specific activity of the mixed serum proteins increased almost linearly. From the rate of increase and the specific activity of the free lysine at plateau, an approximate estimate can be made of the renewal rate of the serum proteins. This estimate must be too low, because the specific activity of the free amino acid at the site of synthesis, e.g. in the liver cell, must always be lower than in serum. The validity of the continuous infusion method is discussed in relation to other methods of measuring total amino acid or protein turnover.(AU)
Responsável: JM3.1 - Médical Library
JM3.1; RC31.C56


  3 / 12 MedCarib  
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Fotocópia
Id: 15822
Autor: Waterlow, John C.
Título: Observations on the mechanism of adaptation to low protein intakes
Fonte: Lancet;2(578):1091-7, 23, Nov. 1968.
Idioma: En.
Responsável: JM3.1 - Médical Library
JM3.1; R31.L3


  4 / 12 MedCarib  
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Fotocópia
Id: 14624
Autor: Waterlow, John C; Stephen, Joan M. L.
Título: The effect of low protein diets on the turn-over rates of serum, liver and muscle proteins in the rat, measured by continuous infusion of L-[14C]lysine
Fonte: Clin Sci;35(2):287-305, Oct. 1968.
Idioma: En.
Responsável: JM3.1 - Médical Library
JM3.1; R31.C56


  5 / 12 MedCarib  
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Fotocópia
Id: 14365
Autor: Waterlow, John C; Stephen, Joan M. L.
Título: Adaptation of the rat to a low-protein diet: the effect of a reduced protein intake on the pattern of incorporation of L-[14C] lysine
Fonte: Br J Nutr;20(3):461-84, 1966.
Idioma: En.
Responsável: JM3.1 - Médical Library
JM9.1; QP141.A1B7


  6 / 12 MedCarib  
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Fotocópia
Id: 14350
Autor: Turner, L. V; Manchester, Keith L.
Título: Effects of denervation hypertrophy in rat diaphragm muscle on the activity of ribosomes and sap fractions in protein synthesis
Fonte: Biochim Biophys Acta;299(4):612-20, Apr 11, 1973.
Idioma: En.
Responsável: JM3.1 - Médical Library
JM9.1; QP501.B56


  7 / 12 MedCarib  
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Fotocópia
Id: 12243
Autor: Neale, R. J.
Título: Aminoacid absorption in protein malnutrition - letter
Fonte: Lancet;1(690):143, Jan. 16 1971.
Idioma: En.
Responsável: JM3.1 - Médical Library
JM3.1; R31.L3


  8 / 12 MedCarib  
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Fotocópia
Id: 10978
Autor: Wilson, Murchison B; Morck, I. L.
Título: Influence of ribinucleic acid from inflammatory leukocytes of C14 glycine into protein by bone marrow and thymus cells
Fonte: West Indian med. j;20(2):83-6, June 1971.
Idioma: En.
Responsável: JM3.1 - Médical Library
JM3.1; R18.W4


  9 / 12 MedCarib  
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Fotocópia
Id: 10194
Autor: Millward, David J.
Título: Protein turnover in skeletal muscle. I. The effect of starvation and a protein-free diet on the synthesis and catabolism of skeletal muscle proteins in comparison to liver
Fonte: Clin Sci;39(5):591-603, 1970. tab.
Idioma: En.
Resumo: Rates of synthesis and catabolism of liver and muscle sarcoplasmic and myofibrillar protein have been measured in young control, starved and protein (deprived) rats using [14C]Na2CO3 to label protein. Half-lives for synthesis of 1.35, 2.8 and 7.2 days for liver, sarcoplasmic and myofibrillar proteins, respectively were obtained, whilst half-lives for catabolism were 1.55, 3.6 and 15.6 days in each case in the control animals. The protein free diet for 3 days caused a small decrease in the rate of synthesis of liver and muscle proteins. The catabolic rate of liver protein was increased by 20 percent whilst there was a smaller increase in the catabolic rate of myofibrillar proteins. Starvation for 3 days caused a 20 percent reduction in the rate of liver protein synthesis whilst there were greater reductions in muscle protein synthesis. The catabolic rate of liver protein was only slightly increased whereas there was a 75 percent increase in the rate of myofibrillar protein breakdown. The total amount of protein synthesis and catabolism in liver and the 2 muscle protein fractions over the first 3 days of the 3 regimes were calculated. Muscle protein turnover, in particular myofibrillar, was shown to be very sensitive to dietary protein and/or calorie deficiency. These results are discussed in terms of the mobility and therefore importance of muscle protein metabolism in the economy of the whole animal. (AU)
Responsável: JM3.1 - Médical Library
JM3.1; R31.C56


  10 / 12 MedCarib  
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Fotocópia
Id: 8672
Autor: Kean, Eccleston A; Rainford, Ismay J.
Título: Evidence of multiple and independent mechanisms for the action of hypoglycin in vivo
Fonte: Biochem Pharmacol;22(12):1524-6, June 15, 1973.
Idioma: En.
Responsável: JM9.1
JM9.1; QP901.B5



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