Purification of plant mitochondria by isopycnic centrifugation in density gradients of Percoll

Neuburger, Michel; Journet, Etienne-Pascal; Bligny, Richard; Carde, Jean‐Pierre; Douce, Roland

doi:10.1016/0003-9861(82)90507-0

Cited by 316 publications

(205 citation statements)

References 18 publications

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“…Electron micrographs of spinach leaf mitochondria have been published elsewhere [15]. Oxygen uptake of the fractions was in the range of 460nmol 0, x min-' x mg protein-' and, thus, in accordance with published values [16].…”

Section: Characterization Of the Isolated Mitochondriasupporting

confidence: 84%

On the biosynthesis of ubiquinones in plant mitochondria

1984

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Isolated mitochondria from potato tubers, spinach leaves, and daffodil petals form intermediates of the ubiqujnone biosynthetic pathway (prenylated 4-hydroxybenzoate, prenylated phenols, and quinoid compounds) from [l -lSC]isopentenyl diphosphate and endogcnous or exogenous 4-hydroxybenzoate. In contrast [2-'4C]mevalonate 5-diphosphate, the immediate precursor of isopentenyl diphosphate was not accepted as a substrate. These results suggest that plant mitochondria have their own prenyltransferase and prenylation system, similar to the plastid compartment which also starts by the use of isopentenyl diphosphate [see Kreuz, K. and Kleinig, H. (1984) Eur. J. BiocArm. 141,

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Section: Characterization Of the Isolated Mitochondriasupporting

confidence: 84%

On the biosynthesis of ubiquinones in plant mitochondria

1984

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“…In contrast, the activities of the peroxisomal enzyme markers catalase, urate oxidase, and ACOX were decreased 7-to 30-fold in the course of the purification from the crude organellar extract to Percoll-purified mitochondria (Dieuaide et al, 1993). The removal of peroxisomal enzyme markers during this purification was comparable with that obtained for highly purified mitochondria from potato tuber (Neuburger et al, 1982).…”

Section: Characterization Of Acad Activities Associated With Mitochonsupporting

confidence: 59%

Identification, Separation, and Characterization of Acyl-Coenzyme A Dehydrogenases Involved in Mitochondrial β-Oxidation in Higher Plants1

Bode

Hooks

Couée³

1999

Plant Physiology

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The existence in higher plants of an additional ␤-oxidation system in mitochondria, besides the well-characterized peroxisomal system, is often considered controversial. Unequivocal demonstration of ␤-oxidation activity in mitochondria should rely on identification of the enzymes specific to mitochondrial ␤-oxidation. Acylcoenzyme A dehydrogenase (ACAD) (EC 1.3.99.2,3) activity was detected in purified mitochondria from maize (Zea mays L.) root tips and from embryonic axes of early-germinating sunflower (Helianthus annuus L.) seeds, using as the enzyme assay the reduction of 2,6-dichlorophenolindophenol, with phenazine methosulfate as the intermediate electron carrier. Subcellular fractionation showed that this ACAD activity was associated with mitochondrial fractions. Comparison of ACAD activity in mitochondria and acylcoenzyme A oxidase activity in peroxisomes showed differences of substrate specificities. Embryonic axes of sunflower seeds were used as starting material for the purification of ACADs. Two distinct ACADs, with medium-chain and long-chain substrate specificities, respectively, were separated by their chromatographic behavior, which was similar to that of mammalian ACADs. The characterization of these ACADs is discussed in relation to the identification of expressed sequenced tags corresponding to ACADs in cDNA sequence analysis projects and with the potential roles of mitochondrial ␤-oxidation in higher plants.

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“…The modulator activity was found in the supernatant. The modulator was also obtained from mitochondria purified on percoll gradients using the procedure for potato mitochondria [9].…”

Section: Methodsmentioning

confidence: 99%

The mitochondrial outer membrane channel, VDAC, is modulated by a soluble protein

Holden

Colombini

1988

FEBS Letters

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The mitochondrial outer membrane channel, VDAC, serves as the primary permeability pathway for metabolite flux between cytoplasmic and mitochondrial compartments. VDAC can occupy several conformational states differing in ion conductivity. Small transmembrane potentials cause transitions from open-to closed-channel conformations. A soluble mitochondrial protein enhances the channel's response to voltage by increasing the rate of channel closing; inducing the occupation of lower conductance states; and decreasing the rate of channel reopening. This protein modulator acts at very low concentrations and its role in the cell may be to regulate the permeability of the mitochondrial outer membrane by inducing channel closure.

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Purification of plant mitochondria by isopycnic centrifugation in density gradients of Percoll

Cited by 316 publications

References 18 publications

On the biosynthesis of ubiquinones in plant mitochondria

On the biosynthesis of ubiquinones in plant mitochondria

Identification, Separation, and Characterization of Acyl-Coenzyme A Dehydrogenases Involved in Mitochondrial β-Oxidation in Higher Plants1

The mitochondrial outer membrane channel, VDAC, is modulated by a soluble protein

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