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G Lutze1, W Liese, W Kunz

  • 1Physiol.-chem. Institut der Medizinischen Akademie Magdeburg, 301, Magdeburg, DDR

FEBS Letters
|August 1, 1972
PubMed
Summary
This summary is machine-generated.

Mitochondria facilitate an energy-independent exchange of alkali metal cations for protons, with varying affinities. Disintegration reveals more proton release sites, suggesting inner membrane accessibility changes.

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Area of Science:

  • Mitochondrial physiology
  • Ion transport mechanisms

Background:

  • Mitochondria play a crucial role in cellular energy metabolism.
  • Understanding ion transport is key to mitochondrial function.

Purpose of the Study:

  • To investigate the energy-independent exchange of alkali metal cations for protons in mitochondria.
  • To characterize the specificity and kinetics of this ion exchange process.

Main Methods:

  • Experiments were conducted on both intact and disintegrated mitochondria.
  • Alkali metal cation exchange against protons was measured under non-energy-dependent conditions.

Main Results:

  • The exchange process was not specific for particular alkali metal ions.
  • In intact mitochondria, apparent K(m) values ranged from 5-25 mM, with maximum proton release of 15-20 nval/mg protein.

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  • Disintegrated mitochondria showed higher proton release (50 nval/mg protein) and no ion specificity, with apparent K(m) around 30 mM.

    • Conclusions:

    • Directly accessible binding sites for alkali metal cations exist in the outer mitochondrial membrane.
    • Inner mitochondrial membrane binding sites are accessible only after mitochondrial disintegration, indicating a role for membrane integrity.