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STRUCTURE AND MODE OF ACTION OF A VOLTAGE DEPENDENT ANION‐SELECTIVE CHANNEL (VDAC) LOCATED IN THE OUTER MITOCHONDRIAL MEMBRANE DEPENDENT ANION‐SELECTIVE CHANNEL (VDAC) *
Author(s) -
Colombini Marco
Publication year - 1980
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1980.tb47198.x
Subject(s) - voltage dependent anion channel , porin , bacterial outer membrane , chemistry , biophysics , ion channel , membrane , lipid bilayer , permeability (electromagnetism) , ion , biochemistry , biology , escherichia coli , receptor , organic chemistry , gene
VDAC is a channel-forming protein, located in the outer mitochondrial membrane, whose properties are consistent with the known permeability behavior of that membrane. When extracted with Triton X-100, VDAC exists as a 110,000 molecular weight glycoprotein complex which is a prepackaged channel. When inserted into liposomes, the permeability increase to non-electrolytes is consistent with a pore radius of 20. In a planar lipid bilayer, VDAC is anion selective and voltage gatable. This suggests that the permeability pathway in the outer mitochondrial membrane might be under physiological control. Many of VDAC's properties are qualitatively very similar, although quantitatively different, to those of porin, the channel responsible for the permeability of the outer membrane of at least some gram negative bacteria.