Aug 1, 1989

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

Journal of Bioenergetics and Biomembranes
F Palmieri, V De Pinto


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 head-group 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.

Mentioned in this Paper

Mitochondria, Heart
Porin Activity
Ion Channel
Voltage-Dependent Anion Channels
Purification Aspects
Intracellular Membranes
Pore Proteins
Hydroxyapatite Arthropathy

About this Paper

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