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- W2085035915 abstract "The outer mitochondrial membrane porin, voltage-dependent anion-selective channel (VDAC), is believed to play an important role in mediating mitochondria-dependent apoptosis. However, detailed structure-function studies of VDAC have been hindered by the difficulties to obtain a soluble, correctly folded, and fully active form of the recombinant VDAC and its mutant variants due to its transmembrane nature. Here we report a high-throughput one-step chromatographic procedure in purification of recombinant human VDAC1 (rhVDAC1) protein overexpressed in bacteria. The improved methodology could generate a large quantity of rhVDAC1 with correct folding in terms of the secondary structure, with full biological activities in mediating cytochrome c release and in interaction with Bcl-X(L). The method will significantly benefit genetic, biochemical, and structural studies of this critical channel protein." @default.
- W2085035915 created "2016-06-24" @default.
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- W2085035915 date "2003-04-01" @default.
- W2085035915 modified "2023-10-16" @default.
- W2085035915 title "One-step on-column affinity refolding purification and functional analysis of recombinant human VDAC1" @default.
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- W2085035915 doi "https://doi.org/10.1016/s0006-291x(03)00359-0" @default.
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