Purification of VDAC1 from rat liver mitochondria.

Danya Ben-Hail, Varda Shoshan-Barmatz

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

To make biophysical measurements of functions such as the pore-forming activity of mitochondrial voltage-dependent anion-selective channel protein 1 (VDAC1), it is first necessary to obtain a source of purified VDAC protein. In this protocol, we present a method for obtaining rat liver mitochondria as a source of VDAC1 and then describe two methods, one using a nonionic detergent and the other an ionic detergent, for purifying VDAC1 from the isolated mitochondria. This produces a source of VDAC1 proteins that are suitable for subsequent incorporation into artificially prepared phospholipid bilayers. Furthermore, the isolated mitochondria can be used for assaying the mitochondrial permeability transition pore (MPTP).

Original languageEnglish
Pages (from-to)94-99
Number of pages6
JournalCold Spring Harbor Protocols
Volume2014
Issue number1
DOIs
StatePublished - 1 Jan 2014

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology

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