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Acyl Coenzyme A

Acyl Coenzyme A refers to a class of organic compounds consisting of a carboxylic acid joined by a thioester linkage to the sulfhydryl group of coenzyme A.
These molecules play a central role in cellular metabolism, serving as activated acyl groups for biosynthetic reactions, energy production, and signaling pathways.
Acyl CoA species vary in their carbon chain length and degree of saturation, contributing to their diverse biological functions.
Researchers can leverage PubCompare.ai's AI-powered platform to discover effective protocols for studying Acyl Coenzyme A, enhancing the reproducibility and optimization of their research workflows.

Most cited protocols related to «Acyl Coenzyme A»

Cholesterol efflux capacity was quantified in blood samples from the cohort of healthy volunteers as described previously.17 (link) This assay quantifies total efflux mediated by pathways of known relevance in cholesterol efflux from macrophages (i.e., ATP-binding cassette transporter A1 [ABCA1] and G1 [ABCG1], scavenger receptor B1, and aqueous diffusion).17 (link) Each sample was run in triplicate, with a mean coefficient of variation of 4.3%. Values were normalized by dividing the efflux capacity of individual patients by the efflux capacity of a serum pool run with each assay.
Cholesterol efflux capacity in the coronary disease and pharmacologic-study cohorts was quantified with the use of a slightly modified method designed to increase throughput. J774 cells, derived from a murine macrophage cell line, were plated and radiolabeled with 2 μCi of 3H-cholesterol per milliliter. ABCA1 was up-regulated by means of a 6-hour incubation with 0.3 mM 8-(4-chlorophenylthio)-cyclic AMP. Subsequently, efflux mediums containing 2.8% apolipoprotein B–depleted serum were added for 4 hours. All steps were performed in the presence of the acyl–coenzyme A:cholesterol acyltransferase inhibitor CP113,818 (2 μg per milliliter). In a pilot study involving serum samples from 20 healthy volunteers, results from the original assay procedure17 (link) and the modified method were strongly correlated (r = 0.85).
Liquid scintillation counting was used to quantify the efflux of radioactive cholesterol from the cells. The quantity of radioactive cholesterol incorporated into cellular lipids was calculated by means of isopropanol extraction of control wells not exposed to patient serum. Percent efflux was calculated by the following formula: [(microcuries of 3H-cholesterol in mediums containing 2.8% apolipoprotein B–depleted serum – microcuries of 3H-cholesterol in serum-free mediums) ÷ microcuries of 3H-cholesterol in cells extracted before the efflux step] × 100. All assays were performed in duplicate. To correct for interassay variation across plates, a pooled serum control from five healthy volunteers was included on each plate, and values for serum samples from patients were normalized to this pooled value in subsequent analyses. Additional studies that were performed to validate the measurement of cholesterol efflux capacity are described in the Supplementary Appendix.
Publication 2011
ABCA1 protein, human ABCG1 protein, human Acyl Coenzyme A Apolipoproteins B Biological Assay BLOOD Cell Lines Cells Cholesterol Culture Media Cyclic AMP Diffusion Healthy Volunteers Heart Disease, Coronary Isopropyl Alcohol Lipids Macrophage Mus Patients Radioactivity Scavenger Receptor Serum Sterol O-Acyltransferase
Acyl-CoA extraction was performed as previously described[20 (link)] after spiking in 100 μL of acyl-CoA internal standards derived from pan6 deficient Saccharomyces cerevisiae grown in [13C315N1]-pantothenic acid containing media as previously described[21 (link)]. Since this acyl-CoA internal standard is biologically derived, some batch to batch variation is expected, but our previous calculations on yield estimate 100 μL of acyl-CoA internal standards produced by this method to contain 200 ng of [13C315N1]-acetyl-CoA, 20 ng of [13C315N1]-succinyl-CoA, and 5 ng of [13C315N1]-propionyl-CoA as well as varying amounts of other [13C315N1]-acyl-CoAs not included in this study.
Publication 2016
Acyl Coenzyme A Coenzyme A, Acetyl Pantothenic Acid propionyl-coenzyme A Saccharomyces cerevisiae succinyl-coenzyme A

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Publication 2016
3-Hydroxybutyrate Acids acylcarnitine Acyl Coenzyme A Amino Acids BLOOD Capillaries Cholesterol Diagnosis Electrons Fatty Acids, Esterified Gas Chromatography-Mass Spectrometry Glycerin Isoleucine Isotopes Keto Acids Ketogenic Diet Ketones Lactates Leucine Liver Muscle, Gastrocnemius Plasma Tandem Mass Spectrometry Technique, Dilution Triglycerides Valine
Acyl-CoAs were analyzed on an Ultimate 3000 Quaternary UHPLC coupled to a Q Exactive Plus mass spectrometer operating in the positive ion mode with a heated ESI probe in an IonMax Source housing. Samples were kept in a temperature controlled autosampler at 6 °C and LC separation was performed as previously described on a Waters XBridge 3.5 μm particle size C18 2.1 × 150 mm column. LC conditions were as follows modified from previous studies[22 (link), 20 (link)]; column oven temperature 25 °C, solvent A water with 5 mM ammonium acetate, solvent B 95:5 acetonitrile: water with 5 mM ammonium acetate, solvent C (wash solvent) 80:20 acetonitrile: water with 0.1% formic acid. The gradient was as follows: 0.2 mL/min flow at 98% A and 2% B for 1.5 min, 80% A 20% B at 5 min, 100% B at 12 min, 0.3 mL/min 100% B at 16 min, 0.2 mL/min 100% C at 17 min, held to 21 min, then re-equilibrated at 0.2 mL/min flow at 98% A and 2% B from 22 to 28 min. Flow from 4–18 minutes was diverted to the instrument. Operating conditions on the mass spectrometer were as follows; auxiliary gas 10 arbitrary units (arb), sheath gas 35 arb, sweep gas 2 arb, spray voltage 4.5 kV, capillary temperature 425 °C, S-lens RF-level 50, aux gas heater temperature 400 °C, in-source CID 5 eV. Scan parameters were optimized during the experiments, but final conditions were alternating full scan from 760–1800 m/z at 140,000 resolution and data independent acquisition (DIA) looped 3 times with all fragment ions multiplexed at a normalized collision energy (NCE) of 20 at a resolution of 280,000. An isolation width of 7 m/z with an offset of 3 m/z was used to capture all relevant isotopologues for targeted acyl-CoAs. Data was processed in Xcalibur, TraceFinder (Thermo), and then isotopic enrichment was calculated by the method of Fernandez, et al., to compensate for the non-linearity of isotopic enrichment[23 (link)]. Statistical analysis and graphical plots were generated in Prism v6 (GraphPad, LaJolla, CA). Using these conditions, we re-validated the precision of this LC-MS/HRMS method for acyl-CoAs. We conducted validation for inter- (n=3) and intra-day (n=3) precision for low (LQC), medium (MQC) and high quality control (HQC) levels of 12.5, 50, and 250 ng on column, respectively. Co-efficient of variation (inter-/intra-day) for LQC, MQC, and HQC of acetyl-CoA were 16.9%/16.1%, 2.7%/6.2%, 18.2%/13.5%, respectively. Values for succinyl-, propionyl- and other short chain acyl-CoAs were likewise below 20% for inter- and intra-day variation.
Publication 2016
acetonitrile Acyl Coenzyme A ammonium acetate ARID1A protein, human Capillaries Coenzyme A, Acetyl formic acid Ions isolation Isotopes Lens, Crystalline prisma Radionuclide Imaging Solvents

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Publication 2015
Acyl Coenzyme A Coenzyme A, Acetyl Freezing Yeasts

Most recents protocols related to «Acyl Coenzyme A»

A selection of
sublethal end points related to, e.g., neurological impacts, lipid
metabolism, and oxidative responses of shrimp were addressed in the
study. Validated protocols were used to analyze the following parameters:
acetylcholinesterase activity (AChE) in gills and muscle tissues to
assess neurotoxicity; AcylCoA (acyl coenzyme A) oxidase activity (ACOX),
involved in different aspects of lipid homeostasis in the digestive
gland; antioxidant response and oxidative damage in digestive gland
by total oxyradical scavenging capacity (TOSC assay toward peroxyl
and hydroxyl radicals); and lipid peroxidation (malondialdehyde levels).
The parameters described above were analyzed in tissues at the end
of exposure (day 4) and at the end of the recovery period (day 14).
Analytical methods are described in the SI.
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Publication 2023
Acetylcholinesterase Acyl CoA Oxidase Acyl Coenzyme A Antioxidants Biological Assay Digestive System Gills Homeostasis Hydroxyl Radical Lipid Peroxidation Lipids Malondialdehyde Muscle Tissue Neurotoxicity Syndromes Oxidative Damage Pain Tissues

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Publication 2023
Acyl Coenzyme A ammonium acetate cDNA Library Cells Centrifugation Chromatography, Reversed-Phase Liquid Dry Ice Genotype Intestinal Atresia, Multiple K562 Cells Lyase Malonyl Coenzyme A Nitrogen Normal Saline Radionuclide Imaging Retention (Psychology) Saline Solution Vacuum

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Publication 2023
Acyl CoA Oxidase Acyl Coenzyme A BLOOD Blood Glucose Body Weight Cholesterol Enzyme-Linked Immunosorbent Assay Enzyme Assays Fluorescence Glucose Hydroxybutyrates Immune Tolerance Injections, Intraperitoneal Insulin Mice, Inbred NOD Mus Nitric Oxide Synthase Nonesterified Fatty Acids Plasma Randox Serum Tail Technique, Dilution Triglycerides
Acyl-CoA synthase activity was measured in 10–30 µg of cellular lysates from differentiated cells using 50 µM of 1-14C-palmitate (specific activity 0.1 µCi/µL) for 5 min at 37 °C as described in [45 (link)]. The reaction was terminated by the addition of 1ml of Dole’s reagent and centrifugation at 1000× g for 3 min. The lower layer was washed twice in 2 mL of heptane and counted in 4 mL of scintillation cocktail. Data were normalized to protein content.
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Publication 2023
Acyl Coenzyme A Cells Centrifugation Heptane Nitric Oxide Synthase Proteins vitamin A palmitate

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Publication 2023
Acyl Coenzyme A Amino Acids benzoyl-coenzyme A Biological Assay Dithionitrobenzoic Acid enzyme activity Enzymes Ethanol Glutamine Glycine isovaleryl-coenzyme A Kinetics phenylacetyl-coenzyme A Recombinant Proteins Technique, Dilution Tissue, Membrane Tromethamine Tungsten

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Acyl-CoAs are a class of organic compounds that serve as important intermediates in various metabolic pathways, including fatty acid metabolism and energy production. These molecules are composed of a fatty acid chain attached to the coenzyme A (CoA) group. Acyl-CoAs play a crucial role in the process of beta-oxidation, where they are used as substrates for the breakdown of fatty acids to generate energy for the cell.
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The Q Exactive Plus is a high-resolution, accurate-mass Orbitrap mass spectrometer designed for a wide range of applications, including proteomics, metabolomics, and small molecule analysis. It features high-performance mass analysis, with a mass resolution up to 280,000 FWHM at m/z 200 and mass accuracy of less than 1 ppm.
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T4 DNA ligase is an enzyme that catalyzes the formation of phosphodiester bonds between adjacent 3'-hydroxyl and 5'-phosphate termini in DNA. It is commonly used in molecular biology for the joining of DNA fragments.
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Acyl-CoAs are a group of essential cofactors involved in various metabolic processes. They serve as the activated form of fatty acids, playing a crucial role in lipid biosynthesis and energy production within cells.
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The Thermo Scientific™ Ultimate 3000 is a high-performance liquid chromatography (HPLC) system designed for a wide range of analytical applications. It features a modular design, allowing for customization to meet specific laboratory needs.
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Palmitoyl-CoA is a coenzyme A thioester that serves as a key intermediate in lipid metabolism and biosynthesis. It is produced by the enzyme palmitoyl-CoA synthetase and acts as a substrate in various enzymatic reactions, including fatty acid elongation and beta-oxidation.
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[3H]-cholesterol is a radioactively labeled form of cholesterol, containing the tritium (3H) isotope. It is used as a tracer in various research applications to study cholesterol metabolism and related biological processes.
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More about "Acyl Coenzyme A"

Acyl Coenzyme A (Acyl-CoA) refers to a class of organic compounds consisting of a carboxylic acid joined by a thioester linkage to the sulfhydryl group of coenzyme A.
These molecules play a central role in cellular metabolism, serving as activated acyl groups for biosynthetic reactions, energy production, and signaling pathways.
Acyl-CoA species vary in their carbon chain length and degree of saturation, contributing to their diverse biological functions.
Researchers can leverage PubCompare.ai's AI-powered platform to discover effective protocols for studying Acyl-CoAs, enhancing the reproducibility and optimization of their research workflows.
By accessing the vast repository of research literature, pre-prints, and patents, researchers can locate the best protocols for their specific needs, using data-driven comparisons to ensure their research is built on the most effective and reliable methods.
Acyl-CoAs are central to a variety of cellular processes, including fatty acid metabolism, protein modification, and energy production.
Techniques such as Q Exactive Plus mass spectrometry, T4 DNA ligase, and Ultimate 3000 HPLC systems are commonly used to analyze and quantify Acyl-CoA species, such as Palmitoyl-CoA and [3H]-cholesterol.
Additionally, software like SigmaPlot 12.5 can be employed for data analysis and visualization, while Trichloroacetic acid and Oasis HLB 1cc (30 mg) SPE columns are used for sample preparation and purification.
By understanding the role of Acyl-CoAs in cellular metabolism and leveraging the power of PubCompare.ai, researchers can optimze their workflows, enhance the reproducibility of their studies, and uncover the most effective protocols for their Acyl-CoA research.