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  • 1
    Electronic Resource
    Electronic Resource
    Kinetic properties of the potassium/hydrogen ion antiport of heart mitochondria (1990)
    s.l. : American Chemical Society
    Biochemistry 29 (1990), S. 408-415 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00454a015
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  • 2
    Electronic Resource
    Electronic Resource
    Matrix free magnesium changes with metabolic state in isolated heart mitochondria (1990)
    s.l. : American Chemical Society
    Biochemistry 29 (1990), S. 4121-4128 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00469a015
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  • 3
    Electronic Resource
    Electronic Resource
    Structural perturbation of the a3-CuB site in mitochondrial cytochrome c oxidase by alcohol solvents (1990)
    s.l. : American Chemical Society
    Biochemistry 29 (1990), S. 4627-4633 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00471a018
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  • 4
    Electronic Resource
    Electronic Resource
    Kinetic properties of the sodium/hydrogen ion antiport of heart mitochondria (1989)
    s.l. : American Chemical Society
    Biochemistry 28 (1989), S. 4347-4354 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00436a034
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  • 5
    Electronic Resource
    Electronic Resource
    Properties of the Na+-Ca2+ Antiport of Heart Mitochondriaa (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 779 (1996), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1996.tb44836.x
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  • 6
    Electronic Resource
    Electronic Resource
    Induction of Na+ / K+ exchange in swollen heart mitochondria (1980)
    Springer
    Journal of bioenergetics and biomembranes 12 (1980), S. 233-247 
    Details
    ISSN: 1573-6881
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Heart mitochondria swollen passively in nitrate salts contract in a respiration-dependent reaction which can be attributed to an endogenous cation/H+ exchange component (or components). The rate of contraction increases with increased extent of passive swelling in both Na+ and K+ salts. Since nearly constant internal cation concentrations are maintained during osmotic swelling, this result suggests that both Na+/H+ and K+/H+ exchange is enhanced by increased matrix volume. Endogenous Mg2+ is also lost with increased matrix volume, and this observation, in conjunction with other evidence available in the literature, suggests that monovalent cation/H+ exchanges may be regulated by divalent cations. Passive exchange of Na+/K+,42K+/K+, and24Na+/Na+ can be readily demonstrated in mitochondria swollen in nitrate. All these exchanges are low or not detectable in unswollen control mitochondria, and it appears that they are manifestations of the activated cation/H+ component (or components) functioning in the absence of ΔpH.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00744686
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  • 7
    Electronic Resource
    Electronic Resource
    Effects of quinine on K+ transport in heart mitochondria (1984)
    Springer
    Journal of bioenergetics and biomembranes 16 (1984), S. 379-390 
    Details
    ISSN: 1573-6881
    Keywords: Quinine ; quinacrine ; mitochondrial K+/H+ antiport ; swelling and contraction of heart mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Quinine inhibits the respiration-dependent extrusion of K+ from Mg2+-depleted heart mitochondria and the passive osmotic swelling of these mitochondria in K+ and Na+ acetate at alkaline pH. These observations concur with those of Nakashima and Garlid (J. Biol. Chem. 257, 9252, 1982) using rat liver mitochondria. Quinine also inhibits the respiration-dependent contraction of heart mitochondria swollen passively in Na+ or K+ nitrate and the increment of elevated respiration associated with the extrusion of ions from these mitochondria. Quinine, at concentrations up to 0.5 mM, inhibits the respiration-dependent42K+/K+ exchange seen in the presence of mersalyl, but higher levels of the drug produce increased membrane permeability and net K+ loss from the matrix. These results are all consistent with an inhibition of the putative mitochondrial K+/H+ antiport by quinine. However, quinine has other effects on the mitochondrial membrane, and possible alternatives to this interpretation are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00743233
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  • 8
    Electronic Resource
    Electronic Resource
    Respiration-dependent contraction of swollen heart mitochondria: Participation of the K+/H+ antiporter (1988)
    Springer
    Journal of bioenergetics and biomembranes 20 (1988), S. 229-242 
    Details
    ISSN: 1573-6881
    Keywords: K+/H+ antiport ; mitochondria ; mitochondrial contraction ; dicyclohexylcarbodiimide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Respiration-dependent contraction of heart mitochondria swollen passively in K+ nitrate is activated by the ionophore A23187 and inhibited by Mg2+. Ion extrusion and osmotic contraction under these conditions are strongly inhibited by quinine, a known inhibitor of the mitochondrial K+/H+ antiporter, as measured in other systems. The inhibition by quinine is relieved by the exogenous antiporter nigericin. Respiration-dependent contraction is also inhibited by dicyclohexylcarbodiimide (DCCD) when reacted under conditions known to inhibit K+/H+ antiport (Martinet al., J. Biol. Chem. 259, 2062–2065, 1984). These studies strongly support the concept that K+ is extruded from the matrix by the endogenous K+/H+ antiporter and that inhibition of this component by quinine or DCCD inhibits respiration-dependent contraction. The extrusion of K+ nitrate is accompanied by a respiration-dependent efflux of a considerable portion of the endogenous Mg2+. This Mg2+ efflux does not occur in the presence of nigericin or when the mitochondrial Na+/H+ antiporter is active. Mg2+ efflux may take place on the K+/H+ antiporter. DCCD, reacted under conditions that do not result in inhibition of the K+/H+ antiporter, blocks a monovalent cation uniport pathway. This uniport contributes to futile cation cycling at elevated pH, and its inhibition by DCCD stimulates respiration-dependent contraction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00768396
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  • 9
    Electronic Resource
    Electronic Resource
    Inhibition of the Na+/Ca2+ antiport of heart mitochondria by diethylpyrocarbonate (1987)
    Springer
    Journal of bioenergetics and biomembranes 19 (1987), S. 515-524 
    Details
    ISSN: 1573-6881
    Keywords: Mitochondria ; diethylpyrocarbonate ; heart ; inhibition ; sodium ; calcium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Diethylpyrocarbonate inhibits Na+/Ca2+ antiport activity in isolated heart mitochondria. The inhibition is time-dependent with maximum activity developed after 5 min at 25°C. The reaction of diethylpyrocarbonate with the mitochondrial membrane is biphasic with 25–30 nmol mg−1 reacting rapidly and an additional 30 nmol mg−1 taken up slowly over a 30-min incubation. Inhibition of mitochondrial Na+/Ca2+ antiport by diethylpyrocarbonate decreases theV max of the reaction, and the inhibition cannot be reversed by washing the mitochondria or addition of excess histidine. The inhibition occurs at levels of inhibitor that have little or no effect on Ca2+ uptake, Na+/H+ antiport, or succinate respiration. A portion of the Na+-dependent efflux of Ca2+ is insensitive to diethylpyrocarbonate and this component is abolished by diltiazem. The mechanism by which diethylpyrocarbonate inactivates Na+/Ca2+ antiport is still uncertain, but may involve the modification of an unprotonated histidine residue in the transporter.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00770034
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  • 10
    Electronic Resource
    Electronic Resource
    K+/H+ antiport in mitochondria (1988)
    Springer
    Journal of bioenergetics and biomembranes 20 (1988), S. 193-209 
    Details
    ISSN: 1573-6881
    Keywords: Mitochondria ; K+/H+ antiport ; mitochondrial swelling ; mitochondrial contraction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Mitochondria contain a latent K+/H+ antiporter that is activated by Mg2+-depletion and shows optimal activity in alkaline, hypotonic suspending media. This K+/H+ antiport activity appears responsible for a respiration-dependent extrusion of endogenous K+, for passive swelling in K+ acetate and other media, for a passive exchange of matrix42K+ against external K+, Na+, or Li+, and for the respiration-dependent ion extrusion and osmotic contraction of mitochondria swollen passively in K+ nitrate. K+/H+ antiport is inhibited by quinine and by dicyclohexylcarbodiimide when this reagent is reacted with Mg2+-depleted mitochondria. There is good suggestive evidence that the K+/H+ antiport may serve as the endogenous K+-extruding device of the mitochondrion. There is also considerable experimental support for the concept that the K+/H+ antiport is regulated to prevent futile influx-efflux cycling of K+. However, it is not yet clear whether such regulation depends on matrix free Mg2+, on membrane conformational changes, or other as yet unknown factors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00768394
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