Recombinant Human Voltage Dependent Anion Selective Channel Isoform 3 (hVDAC3) Forms Pores with a Very Small Conductance | Zendy

Vanessa Checchetto | Zendy; Simona Reina | Zendy; Andrea Magrì | Zendy; Ildikò Szabó | Zendy; Vito De Pinto | Zendy

Open Access

Recombinant Human Voltage Dependent Anion Selective Channel Isoform 3 (hVDAC3) Forms Pores with a Very Small Conductance

Author(s) -

Vanessa Checchetto,

Simona Reina,

Andrea Magrì,

Ildikò Szabó,

Vito De Pinto

Publication year - 2014

Publication title -

cellular physiology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.486

H-Index - 87

eISSN - 1421-9778

pISSN - 1015-8987

DOI - 10.1159/000363047

Subject(s) - vdac1 , voltage dependent anion channel , porin , membrane potential , biophysics , chemistry , conductance , recombinant dna , ion channel , membrane , gene isoform , potassium channel , biochemistry , bacterial outer membrane , biology , escherichia coli , receptor , mathematics , combinatorics , gene

Voltage-dependent anion channels (VDAC), also known as eukaryotic porins, are located in the outer mitochondrial membrane and allow the flux of ions and small metabolites. While the pore-forming ability of recombinant VDAC1 and VDAC2 has been extensively studied during the last decades, a clear-cut ion conducting channel activity has not been assigned to the VDAC3 isoform. Methods : Electrophysiological characterization of the recombinant protein purified and refolded was obtained after incorporation into planar lipid bilayers.

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