Purification and properties of the voltage-dependent anion channel of the outer mitochondrial membrane.
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.
Palmieri
F
F
Department of Pharmaco-Biology, University of Bari, Italy.
De Pinto
V
V
D000818:Animals; D003902:Detergents; D007425:Intracellular Membranes / Q000032:analysis; D007473:Ion Channels / Q000032:analysis*; D008565:Membrane Proteins / Q000302:isolation & purification*; D008928:Mitochondria / Q000032:analysis; D008929:Mitochondria, Heart / Q000032:analysis; D018272:Porins; D050994:Voltage-Dependent Anion Channels
D003902:Detergents; D007473:Ion Channels; D008565:Membrane Proteins; D018272:Porins; D050994:Voltage-Dependent Anion Channels