Results 321 to 330 of about 89,018 (342)
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Hereditary and acquired diseases of acyl-coenzyme A metabolism
Molecular Genetics and Metabolism, 2008Coenzyme A (CoA) sequestration, toxicity or redistribution (CASTOR) is predicted to occur in many hereditary and acquired conditions in which the degradation of organic acyl esters of CoA is impaired. The resulting accumulation of CoA esters and reduction of acetyl-CoA and free CoA (CoASH) will then trigger a cascade of reactions leading to clinical ...
Grant A, Mitchell +5 more
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Acyl-Coenzyme A—Cholesterol Acyltransferase Activity in Human Liver
Clinical Science, 19791. In the presence of CoA and ATP, human liver microsomes catalyse the incorporation of [14C]oleate or [14C]cholesterol into cholesteryl oleate, thus demonstrating the presence of acyl-coenzyme A-cholesterol acyltransferase (cholesterol acyltransferase) in human liver. 2. The enzyme has properties similar to those of rat liver enzyme and
Balasubramaniam S +4 more
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Peroxisomal fatty acyl-coenzyme A oxidation in chicken liver
Archives of Biochemistry and Biophysics, 1983The activities of antimycin A-insensitive palmitoyl-CoA oxidation and of palmitoyl-CoA oxidase in peroxisomes from chicken liver were similar to those of rat liver. Catalase and D-amino acid oxidase activities in peroxisomes from chicken liver were lower than those of rat liver, and urate oxidase was not detected.
H, Ishii, S, Ishii, M, Kazama, T, Suga
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Acyl coenzyme A: cholesterol acyltransferase in neonatal chick brain
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1986An acyl coenzyme A:cholesterol acyltransferase activity which directly incorporates palmitoyl coenzyme A into cholesterol esters using endogenous cholesterol as substrate was demonstrated in microsomal preparations from neonatal chick brain. The enzyme showed, at pH 7.4, about 2-fold greater activity than that observed at pH 5.6. Nearly 10-times higher
C, Marco +2 more
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Analytical Biochemistry, 1983
A mixture of Ti(IV) and 4-(2-pyridylazo)resorcinol was found to be useful in the spectrophotometric determination of trace amounts of hydrogen peroxide. The absorbance at 508 nm was proportional to the concentration of hydrogen peroxide added. The reagent was successfully applied to the assay of free fatty acid in serum through the combined use of acyl-
C, Matsubara +3 more
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A mixture of Ti(IV) and 4-(2-pyridylazo)resorcinol was found to be useful in the spectrophotometric determination of trace amounts of hydrogen peroxide. The absorbance at 508 nm was proportional to the concentration of hydrogen peroxide added. The reagent was successfully applied to the assay of free fatty acid in serum through the combined use of acyl-
C, Matsubara +3 more
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Medium chain acyl-coenzyme A dehydrogenase deficiency.
New Jersey medicine : the journal of the Medical Society of New Jersey, 1992Medium chain acyl-coenzyme A dehydrogenase deficiency (MCADD) was the first metabolic disorder found to be associated with sudden infant death syndrome. This review covers recent advances in the biochemical and molecular understanding of MCADD.
M J, Bennett, D E, Hale
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Short-Chain Acyl-Coenzyme A Synthetases in Rhodopseudomonas sphaeroides
The Journal of Biochemistry, 1982Two short-chain fatty acyl-CoA synthetases were extracted from the photosynthetic bacterium, Rhodopseudomonas sphaeroides, and partially purified by column chromatography on Sephacryl S-200 and DEAE-cellulose. One enzyme activated propionate, valerate, acrylate, butyrate, and acetate, and was designated as propionyl-CoA synthetase, since the highest ...
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15 Acyl Coenzyme A: Cholesterol O-Acyltransferase
1983Publisher Summary This chapter focuses on Acyl coenzyme A: cholesterol O -acyltransferase (ACAT), which utilizes long-chain fatty acyl coenzyme A and cholesterol as substrates to catalyze the formation of cholesterol esters. This enzyme is responsible for the cellular synthesis of cholesterol esters in various cell types. The presence of cholesterol-
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Effect of ethanol on hepatic acyl-coenzyme A metabolism
Archives of Biochemistry and Biophysics, 1965Abstract Ethanol feeding to fed or fasted rats lowers the hepatic concentration of long chain acyl-CoA derivatives, despite large increases in hepatic triglyceride content. This effect is limited to the duration of ethanol metabolism and is associated with an increase in hepatic α-glycerolphosphate concentration.
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