Identification and purification of a peroxisomal branched chain fatty acyl-CoA oxidase.

Veldhoven, Paul P. Van; Vanhove, Geertrui F.; Vanhoutte, Filip; Dacremont, Georges; Parmentier, G.; Eyssen, H.; Mannaerts, Guy P.

doi:10.1016/s0021-9258(18)54283-6

Cited by 78 publications

(8 citation statements)

References 26 publications

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“…Hiload 16/60 Superdex-200 gel-filtration column, HiTrap chelating affinity columns (5 ml) and palmitoyl-CoA were purchased from Pharmacia Belga, Brussels, Belgium. Hydroxyapatite columns (Econo-Pac HTP cartridge; 5 ml) were from Bio-Rad, Richmond, CA, U.S.A. THC-CoA [6], (±)-2-methylpalmitoyl-CoA [7], pristanoyl-CoA [7] and (± )-2-methylhexanoyl-CoA [8] were prepared as described before. Ultrafiltration devices (Centriprep-10 concentrators) were obtained from Grace-Amicon, Beverly, MA, U.S.A.…”

Section: Materials and Methods Materialsmentioning

confidence: 99%

“…Initially, the acyl-CoA oxidases were partially purified from hypotonic rat liver extracts by means of heat treatment in the presence of FAD and (NH4)2SO4 fractionation exactly as described before [7]. In later experiments, the extracts were prepared in a slightly different way.…”

Section: Partially Purffied Oxidase Preparationsmentioning

confidence: 99%

“…of 0.25 M sucrose, 1 mM EDTA, pH 7.2, 0.1 % (v/v) ethanol and centrifuged at 100000 g for 1 h. The pellet was resuspended by means of a Polytron homogenizer in 10 mM pyrophosphate buffer, pH 9.0, 1 mM EDTA, 5 mM benzamidine, 0.5 mM dithiothreitol (DTT), 5 1tM FAD, 0.2 mM phenylmethanesulphonyl fluoride, 0.2 mM tosylphenylalanylchloromethane (5 ml per g of starting liver) and centrifuged again at 100000g. The supernatant was then subjected to heat treatment and (NH4)2SO4 fractionation as described [7], except that all solutions contained in addition 0.5 mM DTT (see below). The partially purified oxidase preparations were stored at -20°C until use.…”

Section: Partially Purffied Oxidase Preparationsmentioning

confidence: 99%

“…The first reaction of peroxisomal f-oxidation is catalysed by an acyl-CoA oxidase, which desaturates an acyl-CoA to a 2-trans-enoyl-CoA and thereby forms hydrogen peroxide. In rat liver, the desaturation of trihydroxycoprostanoyl-CoA (THC-CoA) is catalysed by trihydroxycoprostanoyl-CoA oxidase (THCCox) [5,6], an acyl-CoA oxidase which is different from the recently characterized pristanoyl-CoA oxidase (PCox) [7][8][9] and the well-known palmitoyl-CoA oxidase J [10,11]. The gene of the latter enzyme gives rise, via alternative splicing, to two mRNAs but only one of the oxidases, corresponding to mRNA type I, has been isolated so far [12].…”

Section: Introductionmentioning

confidence: 99%

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Purification and further characterization of peroxisomal trihydroxycoprostanoyl-CoA oxidase from rat liver

Veldhoven

Rompuy

Vanhooren

et al. 1994

Biochemical Journal

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The acyl-CoA oxidase, catalysing the peroxisomal desaturation of the CoA-ester of trihydroxycoprostanic acid, a bile acid intermediate, has been purified to homogeneity from rat liver. Its native molecular mass, as determined by gel filtration and native gel electrophoresis, was 120 and 175 kDa respectively, suggesting a homodimeric protein consisting of 68.6 kDa subunits. If isolated in the presence of FAD, the enzyme showed a typical flavoprotein spectrum and contained most likely 2 mol of FAD per mol of enzyme. The cofactor, however, was loosely bound. The enzyme acted exclusively on 2-methyl-branched compounds, including pristanoyl-CoA and 2-methylhexanoyl-CoA if albumin was present. Important parameters to obtain a pure and active enzyme were the following: (1) using chromatographic separations like hydrophobic interaction and metal affinity, which allow the presence of high salt concentrations, conditions which stabilize the oxidase; (2) avoiding dialysis and (NH4)2SO4 precipitation; (3) including, when appropriate, FAD, dithiothreitol and a diol-compound in the solvents; and (4) carefully monitoring the removal of other acyl-CoA oxidases which possess the same native molecular mass and subunit size.

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Section: Materials and Methods Materialsmentioning

confidence: 99%

Section: Partially Purffied Oxidase Preparationsmentioning

confidence: 99%

Section: Partially Purffied Oxidase Preparationsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Purification and further characterization of peroxisomal trihydroxycoprostanoyl-CoA oxidase from rat liver

Veldhoven

Rompuy

Vanhooren

et al. 1994

Biochemical Journal

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“…Mitochondrial and peroxisomal ␤ -oxidation proceed via similar mechanisms, but the enzymes are different. In human peroxisomes, the first step of ␤ -oxidation, which involves the FAD-dependent dehydrogenation of acyl-CoA esters to their corresponding trans -2-enoyl-CoA esters is catalyzed by two distinct acyl-CoA oxidases (3)(4)(5). One of these oxidases acts on saturated straight-chain acyl-CoA esters with different chain lengths.…”

mentioning

confidence: 99%

Analysis of pristanic acid β-oxidation intermediates in plasma from healthy controls and patients affected with peroxisomal disorders by stable isotope dilution gas chromatography mass spectrometry

Verhoeven

Schor

Struys

et al. 1999

Journal of Lipid Research

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In this paper we report the development of highly sensitive, selective, and accurate stable isotope dilution gas chromatography negative chemical ionization mass spectrometry (GC-NCI-MS) methods for quantification of peroxisomal ␤ -oxidation intermediates of pristanic acid in human plasma: 2,3-pristenic acid, 3-hydroxypristanic acid, and 3-ketopristanic acid. The carboxylic groups of the intermediates were converted into pentafluorobenzyl esters, whereas hydroxyl groups were acetylated and ketogroups were methoximized. Hereafter, the samples were subjected to clean-up by high performance liquid chromatography. Analyses were performed by selected monitoring of the carboxylate anions of the derivatives. Control values of all three metabolites were established (2,3-pristenic acid: 2-48 n m , 3-hydroxypristanic acid: 0.02-0.81 n m , 3-ketopristanic acid: 0.07-1.45 n m ). A correlation between the concentrations of pristanic acid and its intermediates in plasma was found. The diagnostic value of the methods is illustrated by measurements of the intermediates in plasma from patients with peroxisomal disorders. It is shown that in generalized peroxisomal disorders, the absolute concentrations of 2,3pristenic acid, 3-hydroxypristanic acid, and 3-ketopristanic acid were comparable to those in the controls, whereas relative to the pristanic acid concentrations these intermediates were significantly decreased. In bifunctional protein deficiency, elevated levels of 2,3-pristenic acid and 3-hydroxypristanic acid were found. 3-Ketopristanic acid, although within the normal range, was relatively low when compared to the high pristanic acid levels in these patients. -Verhoeven, N. M., D. S. M. Schor, E. A. Struys, E. E. W. Jansen, H. J. ten Brink, R. J. A. Wanders, and C. Jakobs. Analysis of pristanic acid ␤ -oxidation intermediates in plasma from healthy controls and patients affected with peroxisomal disorders by stable isotope dilution gas chromatography mass spectrometry.

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Sequential strategy to identify a susceptibility gene for schizophrenia: Report of potential linkage on chromosome 22q12‐q13.1: Part 1

et al. 1994

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To identify genes responsible for the susceptibility for schizophrenia, and to test the hypothesis that schizophrenia is etiologically heterogeneous, we have studied 39 multiplex families from a systematic sample of schizophrenic patients. Using a complex autosomal dominant model, which considers only those with a diagnosis of schizophrenia or schizoaffective disorder as affected, a random search of the genome for detection of linkage was undertaken. Pairwise linkage analyses suggest a potential linkage (LRH = 34.7 or maximum lod score = 1.54) for one region (22q12-q13.1). Reanalyses, varying parameters in the dominant model, maximized the LRH at 660.7 (maximum lod score 2.82). This finding is of sufficient interest to warrant further investigation through collaborative studies.

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Identification and purification of a peroxisomal branched chain fatty acyl-CoA oxidase.

Cited by 78 publications

References 26 publications

Purification and further characterization of peroxisomal trihydroxycoprostanoyl-CoA oxidase from rat liver

Purification and further characterization of peroxisomal trihydroxycoprostanoyl-CoA oxidase from rat liver

Analysis of pristanic acid β-oxidation intermediates in plasma from healthy controls and patients affected with peroxisomal disorders by stable isotope dilution gas chromatography mass spectrometry

Sequential strategy to identify a susceptibility gene for schizophrenia: Report of potential linkage on chromosome 22q12‐q13.1: Part 1

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