Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: implications for cellular function and mitochondrial structure.

Olaf Stachowiak 1 Uwe Schlattner 1 Max Dolder 1 Théo Wallimann 1
1 Department of Biology
Abstract : The membrane binding properties of cytosolic and mitochondrial creatine kinase isoenzymes are reviewed in this article. Differences between both dimeric and octameric mitochondrial creatine kinase (Mi-CK) attached to membranes and the unbound form are elaborated with respect to possible biological function. The formation of crystalline mitochondrial inclusions under pathological conditions and its possible origin in the membrane attachment capabilities of Mi-CK are discussed. Finally, the implications of these results on mitochondrial energy transduction and structure are presented.
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Article dans une revue
Molecular and Cellular Biochemistry, Springer Verlag, 1998, 184 (1-2), pp.141-51
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http://www.hal.inserm.fr/inserm-00390792
Contributeur : Sarah Hamant <>
Soumis le : mardi 2 juin 2009 - 17:51:00
Dernière modification le : vendredi 12 juin 2009 - 14:10:59

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  • HAL Id : inserm-00390792, version 1
  • PUBMED : 9746318

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Olaf Stachowiak, Uwe Schlattner, Max Dolder, Théo Wallimann. Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: implications for cellular function and mitochondrial structure.. Molecular and Cellular Biochemistry, Springer Verlag, 1998, 184 (1-2), pp.141-51. 〈inserm-00390792〉

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