Results 261 to 270 of about 58,936 (275)
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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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Hyperuricemia in medium-chain acyl-coenzyme A dehydrogenase deficiency
The Journal of Pediatrics, 1992Six infants and children with medium-chain acyl-coenzyme A dehydrogenase deficiency were found to have hyperuricemia during an acute episode. Hyperuricemia may be a clue to the diagnosis of medium-chain acyl-coenzyme A dehydrogenase deficiency.
Carol L. Greene +2 more
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An acyl-coenzyme a dehydrogenase assay utilizing the ferricenium ion
Analytical Biochemistry, 1990A sensitive assay for medium chain acyl-CoA dehydrogenase has been developed by substituting ferricenium hexafluorophosphate for the physiological acceptor, electron transferring flavoprotein. The ferricenium ion is a facile oxidant of the octanoyl-CoA-reduced enzyme with a Vmax of 1400 min-1 and a KM of 55 microM at pH 7.6.
Thomas C. Lehman +3 more
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[50] Acyl coenzyme A-dependent retinol esterification
1990Publisher Summary One of the reactions whereby retinol is esterified for storage in the liver is acyl-CoA-dependent transacylation, catalyzed by the microsomal enzyme acyl-CoA:retinol O-acyltransferase (ARAT). ARAT transfers the acyl group directly from the acyl-CoA derivative to retinol, thereby forming the corresponding retinyl ester.
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The nature of enzyme-substrate complexes in acyl-coenzyme a dehydrogenases
Archives of Biochemistry and Biophysics, 1988The nature of the purple complex formed upon the addition of octanoyl-CoA to the medium chain acyl-CoA dehydrogenase from pig kidney has been addressed by chemical quenching studies. Previous work, using quenching in 0.1 M KOH, suggested that the dehydrogenation product, trans-2-octenoyl-CoA, was not a participant in reduced rat liver enzyme complexes ...
Colin Thorpe, Sze-Mei Lau
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Functional and structural properties of mammalian acyl-coenzyme A thioesterases
Progress in Lipid Research, 2010Acyl-coenzyme A thioesterases (Acots) play important cellular roles in mammalian fatty acid metabolism through modulation of cellular concentrations of activated fatty acyl-CoAs. Acots catalyse the hydrolysis of the thioester bond present within acyl-CoA ester molecules to yield coenzyme A (CoASH) and the corresponding non-esterified fatty acid.
Kirkby, Brenda +4 more
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And then there were acyl coenzyme A:cholesterol acyl transferase inhibitors
Current Opinion in Lipidology, 2006The reputation of acyl coenzyme A:cholesterol acyltransferase (ACAT) inhibitors has changed profoundly from promising new drugs for cardiovascular prevention to drugs without clinical benefits or possibly even with adverse effects.ACAT inhibitors decrease the intracellular conversion of free cholesterol into cholesteryl ester in a number of tissues ...
Erik S.G. Stroes +3 more
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Interactions of acyl-coenzyme A with phosphatidylcholine bilayers and serum albumin
Biochemistry, 1992Interactions of oleoyl- and octanoyl-coenzyme A (CoA) with phosphatidylcholine (PC) vesicles and bovine serum albumin (BSA) were investigated by NMR spectroscopy. Binding of acyl-CoA to small unilamellar PC vesicles and to BSA was detected by changes in 13C and 31P chemical shifts relative to the chemical shifts for aqueous acyl-CoA.
James A. Hamilton, John G. Boylan
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Chain shortening of acyl-coenzyme A by rat liver microsomes
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1972Abstract [9,10-3H]Palmityl-coenzyme A, [9,10-3H]stearyl-coenzyme A and [9,10-3H]-oleoyl-coenzyme A were tested as substrates for shortening the chain by two carbon atoms using liver microsomes from essential fatty acid-deficient rats. The rates of the reaction were 0.87, 0.68 and 0.34 nmole/min per mg microsomal protein, respectively.
Chang Huei-Che, Ralph T. Holman
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[49] Measurement of acyl coenzyme A-dependent esterification of retinol
1990Publisher Summary This chapter presents the method to measure the reaction rate of the acyl-CoA-stimulated esterification of retinol presented to microsomes in dispersed form. This enzymatic reaction is referred to as acyl-CoA: retinol acyltransferase, or ARAT.
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