Hepatic enzymes, CoASH and long-chain acyl-CoA in subcellular fractions as affected by drugs inducing peroxisomes and smooth endoplasmic reticulum.

@article{Berge1983HepaticEC,
  title={Hepatic enzymes, CoASH and long-chain acyl-CoA in subcellular fractions as affected by drugs inducing peroxisomes and smooth endoplasmic reticulum.},
  author={Rolf Kristian Berge and Asle A Aarsland and Olav M. Bakke and Mikael Farstad},
  journal={The International journal of biochemistry},
  year={1983},
  volume={15 2},
  pages={
          191-204
        }
}
Enhancement of long-chain acyl-CoA hydrolase activity in peroxisomes and mitochondria of rat liver by peroxisomal proliferators.
TLDR
The data do not support the proposal that palmitoyl-CoA hydrolase and acid phosphatase belong to the same subcellular particles, and evidence is presented that this activity at least in part, is related to the peroxisomal proliferation.
Fatty acyl-CoA oxidase activity is induced before long-chain acyl-CoA hydrolase activity and acyl-CoA binding protein in liver of rat treated with peroxisome proliferating 3-thia fatty acids.
TLDR
The early accumulation of specific tetradecylthioacetyl-CoA suggests that this ester may be a possible mediator of the induction of fatty acyl- CoA oxidase, which seems to be dependent on a sustained accumulation of total long-chain acyl -CoA esters.
Very Long Chain and Long Chain Acyl-CoA Thioesterases in Rat Liver Mitochondria
TLDR
Comparison of physical and catalytical characteristics of the enzymes studied here and previously purified acyl-CoA thioesterases suggest that M TE-I and MTE-II are novel enzymes.
Effect of choline-deficiency and methotrexate administration on peroxisomal beta-oxidation, palmitoyl-CoA hydrolase activity and the glutathione content in rat liver.
TLDR
The overall results suggest that fat accumulation is not an 'induction signal' for increased peroxisomal beta-oxidation and that choline-deficiency provoked by the CD diet alone increased the reduced glutathione content in liver, whereas MTX did not significantly change this level.
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TLDR
The molecular and catalytic properties of the enzyme suggest that the induced enzyme was different from mitochondrial and microsomal long-chain acyl-CoA hydrolyses in liver.
Dual localization of long-chain acyl-CoA hydrolase in rat liver: one in the microsomes and one in the mitochondrial matrix.
TLDR
Pure matrix and microsomal fractions showed that the two hydrolase activities were differently affected by the presence of divalent cations, and both the specific activity and the saturation concentration of palmitoyl-CoA were higher for theMicrosomal enzyme than for the matrix-associated enzyme.
Differences between microsomal and mitochondrial-matrix palmitoyl-coenzyme A hydrolase, and palmitoyl-L-carnitine hydrolase from rat liver.
TLDR
The data strongly suggest that palmitoyl-CoA hydrolase and palmitOYl-L-carnitine hydrol enzyme are separate microsomal enzymes, and that the hydrolysis of palmitoysl- CoA in the microsome fraction and mitochondria matrix was catalysed by two different enzymes.
Increased biosynthesis of CoA in the liver of rats treated with clofibrate.
TLDR
CoA exerted feed-back inhibition at this step in liver supernatant from normal and clofibrate-treated rats, thought to be the most important factor for the increase of CoA.
Steady-state concentrations of coenzyme A, acetyl-coenzyme A and long-chain fatty acyl-coenzyme A in rat-liver mitochondria oxidizing palmitate.
TLDR
F fluorimetric assays to rat-liver mitochondria oxidizing palmitate in the absence and presence of carnitine indicated two pools of intramitochondrial CoA, which are sensitive to at least 50mumumoles of each and take place without detectable accumulation of acyl-CoA intermediates.
Purification and characterization of long-chain acyl-CoA hydrolase from rat liver mitochondria.
TLDR
It seems likely that serum albumin not only prevents the inhibition of the enzyme by binding the inhibiting micellar form of the substrate, but also stabilizes the enzyme.
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