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Journal of Bioenergetics and Biomembranes

, Volume 21, Issue 4, pp 417-425

Purification and properties of the voltage-dependent anion channel of the outer mitochondrial membrane

  • F. PalmieriAffiliated withDepartment of Pharmaco-Biology, Laboratory of Biochemistry, University of Bari and CNR Unit for the Study of Mitochondria and Bioenergetics
  • , V. De PintoAffiliated withDepartment of Pharmaco-Biology, Laboratory of Biochemistry, University of Bari and CNR Unit for the Study of Mitochondria and Bioenergetics

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Abstract

The methods for the purification of functionally active mitochondrial porin or voltage-dependent anion channel of the outer mitochondrial membrane are critically evaluated. Two rapid and efficient methods are now available. Both make use of a hydroxyapatite/celite column as a single chromatographic step. However, in one method with long polar head-group detergents, porin passes through the column, whereas in the other method, with shorter polar headgroup detergents, porin is first bound to the column and then eluted by the addition of salts. On the basis of these results, a model for the arrangement of porin in the detergent-protein micelles is proposed.

Key Words

Porin VDAC purification LDAO cholesterol reconstitution