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Sensor for free fatty acids based on acyl coenzyme-a synthetase and acyl coenzyme-a oxidase

Analytica Chimica Acta, 1989
Abstract The measurement is based on monitoring dissolved oxgyen consumed by the two sequential reactions catalyzed by the enzymes immobilized in photo-cross-linkable poly (vinyl alcohol) resin (PVA-SbQ). A linear correlation was observed between current decrease and 0.3–2.6 mM oleic or palmitic acid.
Yuko Kameda   +3 more
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[9] Preparation of radioactive acyl coenzyme A

1986
Publisher Summary This chapter discusses the preparation of radioactive acyl coenzyme A. In this procedure, long-chain 14 C-labeled fatty acid is first converted to the acyl chloride by oxalyl chloride, which is then condensed with CoASH to form the corresponding long-chain acyl-CoA.
Amiya K. Hajra, James Bishop
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Fatty Acyl-Coenzyme A Dehydrogenases

Biochemical Society Transactions, 1978
The general enzymology of @-oxidation has suffered extraordinary neglect since the broad outlines of the pathway were established in the 1950’s. For the acyl-CoA dehydrogenases the contributions from the Institute for Enzyme Research at the University of Wisconsin still represent the major part of our knowledge.
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Acyl-coenzyme A: cholesterol acyltransferase family

Frontiers of Biology in China, 2008
The enzymes of the acyl-coenzyme A: cholesterol acyltransferase (ACAT) family are responsible for the in vivo synthesis of neutral lipids. They are potential drug targets for the intervention of atherosclerosis, hyperlipidemia, obesity, type II diabetes and even Alzheimer’s disease.
Zhanyun Guo, Yali Liu
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Hereditary and acquired diseases of acyl-coenzyme A metabolism

Molecular Genetics and Metabolism, 2008
Coenzyme 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
openaire   +3 more sources

[25] Synthesis of nonhydrolyzable acyl-coenzyme A analogs

1997
Publisher Summary This chapter describes the chemical synthesis of different precursors of the nonhydrolyzable acyl–CH2CoA derivatives. The final synthesis of various nonhydrolyzable acyl–CH2CoA derivatives is also described. The activity of pantetheine phosphate adenylyltransferase is assayed in the reverse direction by monitoring the production of ...
Abend, Andreas, Retey, Janos
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Multiple acyl-coenzyme A carboxylases in Pseudomonas citronellolis

Biochemistry, 1976
Pseudomonas citronellolis was shown to contain four different acyl-coenzyme A carboxylases, including acetyl-, propionyl-, 3-methylcrotonyl-, and geranyl-CoA carboxylases, when grown on the appropriate carbon sources. Acetyl-CoA carboxylase activity in crude extracts was stimulated approximately 40-fold by inclusion of 0.4-0.5 M ammonium sulfate in the
Ray Fall, Mina L. Hector
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A spectrophotometric method for the determination of free fatty acid in serum using acyl-coenzyme A synthetase and acyl-coenzyme A oxidase

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-
Yasushi Yoshida   +3 more
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Acyl-Coenzyme A—Cholesterol Acyltransferase Activity in Human Liver

Clinical Science, 1979
1. 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
N. B. Myant   +9 more
openaire   +4 more sources

Inhibition of proline endopeptidase activity by acyl-coenzyme A esters

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
Coenzyme A (CoA), its related compounds and acylcarnitine non-competitively inhibited the activity of proline endopeptidase (PEPase) purified from rat liver cytosol. The degree of inhibition was in the order of acyl-CoA greater than CoA greater than dephospho-CoA greater than or equal to acylcarnitine.
Naomi Yamakawa   +3 more
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