Mitochondrial Oxidations and Energy Coupling

Pullman, Maynard E.; Schatz, G.

doi:10.1146/annurev.bi.36.070167.002543

Cited by 147 publications

(39 citation statements)

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“…Our findings suggest that the stoichiometric of the mitochondrial ATPase system observed for isolated F1 preparations by Lardy and co-workers (see 3,181) occurs also in the complete ATPase system and gives rise to the change of the affinity of the adenine nucleotide acceptor site for ATP and ADP. The differences between the effects of oligomycin and aurovertin that have been well discussed by Ernster, Lee and Jan& [5] may be adequately explained by the fact that oligomycin reacts with the F. component of the system [ 181, which appears to control Vmax, whereas aurovertin reacts with the F, component, which ap pears to control the adenine nucledtide affinities.…”

Section: Resultssupporting

confidence: 63%

Influence of aurovertin on affinity of mitochondrial adenosine triphosphatase for ATP and ADP

Mitchell

Moyle

1970

FEBS Letters

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Section: Resultssupporting

confidence: 63%

Influence of aurovertin on affinity of mitochondrial adenosine triphosphatase for ATP and ADP

Mitchell

Moyle

1970

FEBS Letters

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“…amounts of calcium and inorganic phosphate It has seemed likely, a priori, that the granules (Pullman and Schatz, 1967;Lehninger, 1966). must consist largely of some form of precipitated Concomitantly with the massive accumulation of calcium phosphate, since (a) the calculated interions, large opaque granules are formed inside the nal concentration of calcium and phosphate ions in the mitochondria after maximal uptake greatly exceeds the solubility product for calcium and phosphate, and (b) the electron-opacity of the granules does not depend upon heavy metal staining but is intrinsic.…”

Section: Introductionmentioning

confidence: 99%

Microincineration, Electron Microscopy, and Electron Diffraction of Calcium Phosphate-Loaded Mitochondria

Thomas

Greenawalt

1968

The Journal of Cell Biology

106

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Isolated rat liver mitochondria were incubated in vitro under conditions supporting the massive accumulation of calcium and phosphate. Samples were embedded, thin sectioned, and examined in the electron microscope. The intramitochondrial distribution of insoluble or structure-bound mineral substances was studied by electron microscopy coupled with recently developed techniques of high resolution microincineration. As shown previously, the ion-loaded mitochondria acquire large, internal granules which have inherent electron opacity indicative of high mineral content. Study of ash patterns in preselected areas of sections directly confirmed the high mineral content of the granules, and the appearance of the residues was consistent with the copresence in the granules of some organic material. Other mitochondrial structures were almost devoid of mineral. Thin sections of unincubated control mitochondria also were incinerated. They were found to contain appreciable amounts of intrinsic mineral, seemingly associated with membranes. The normal, dense matrix granules commonly seen in unaltered mitochondria could be seen in intact sections of these control preparations, but after burning no definite correspondence of any ash to the granules could be demonstrated. The normal granules perhaps do not contain mineral. Heating experiments on ash patterns of all the preparations demonstrated the thermal stability and crystallizability of the ash. The crystallized ash of the in vitro-produced dense granules was tentatively shown by electron diffraction to be 3-tricalcium phosphate (whitlockite). This, together with evidence from the literature, suggests that the original, noncrystalline mineral may be a colloidal, subcrystalline precursor of calcium-deficient hydroxyapatite. Experiments were performed on synthetic calcium phosphates for comparison. Other possible applications of the microincineration techniques are briefly discussed.

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“…Thus, it may be that the activity is a consequence of the activity of mitochondria in the production of energy equivalents in the form of ATP from redox energy via a reversible ATPase. This ATPase under the correct conditions can hydrolyze ATP, producing inorganic phosphate (Munn, 1975;Pullman and Schatz, 1967). The possibility exists, therefore, that the residual ATPase activity observed associated with the mitochondrial fraction is due to an endogenous activity rather than a true measure of plasma membrane contamination.…”

Section: Discussionmentioning

confidence: 99%

Isolation of plasma membrane, Golgi apparatus, and endoplasmic reticulum fractions from single homogenates of mouse liver

Croze

Morré

1984

Journal Cellular Physiology

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Procedures to isolate plasma membrane, Golgi apparatus, and endoplasmic reticulum from a single homogenate of mouse liver are described. Fractions contain low levels of contaminating membranes as determined from morphometry and analyses of marker enzymes. The method requires only 2-3 gm of liver as starting material and yields approximately 0.7, 0.7, and 0.5 mg protein/gm liver, respectively, for endoplasmic reticulum, Golgi apparatus, and plasma membrane. Golgi apparatus fractions show high levels of galactosyltransferase activity and consist of cisternal stacks and associated secretory vesicles and tubules. Endoplasmic reticulum fractions are enriched in both glucose-6-phosphatase and nicotinamide adenine dinucleotide phosphate (reduced) (NADPH)-cytochrome c reductase and contain membrane vesicles with attached ribosomes. K+-stimulated p-nitrophenyl phosphatase and (Na+K+) adenosine triphosphatase activity are enriched in the plasma membrane fraction. This fraction consists of membrane sheets, many with junctional complexes, and bile canaliculi that are representative of the total hepatocyte plasma membrane. The fractionation procedure is designed to utilize small amounts of tissue (e.g., with liver slices), to reduce the total time required for fractionation, and to permit comparisons of constituents of plasma membrane, Golgi apparatus, and endoplasmic reticulum prepared from the same starting homogenates.

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Mitochondrial Oxidations and Energy Coupling

Cited by 147 publications

References 0 publications

Influence of aurovertin on affinity of mitochondrial adenosine triphosphatase for ATP and ADP

Influence of aurovertin on affinity of mitochondrial adenosine triphosphatase for ATP and ADP

Microincineration, Electron Microscopy, and Electron Diffraction of Calcium Phosphate-Loaded Mitochondria

Isolation of plasma membrane, Golgi apparatus, and endoplasmic reticulum fractions from single homogenates of mouse liver

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