two dimensional blue native/sds-page to identify mitochondrial complex i subunits modified by 4-hydroxynonenal (hne)
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2015
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Abstract
The lipid peroxidation product 4-hydroxynonenal (HNE) can form protein-linked HNE adducts, thereby impacting protein structure and function. Mitochondrial complex I (NADH-ubiquinone oxidoreductase), containing at least 45 subunits in mammalian cells, sits in a lipid-rich environment and is thus very susceptible to HNE modifications. In this paper, a procedure for the identification of HNE-modified complex I subunits is described. Complex I was isolated by first dimensional nongradient blue native polyacrylamide gel electrophoresis (BN-PAGE). The isolated complex I band, visualized by either Coomassie blue staining or silver staining, was further analyzed by second dimensional SDS-PAGE. HNE-modified proteins were visualized by Western blotting probed with anti-HNE antibodies. HNE-positive bands were then excised and the proteins contained in them were identified by mass spectrometric peptide sequencing. The method was successfully applied for the identification of two complex I subunits that showed enhanced HNE-modifications in diabetic kidney mitochondria.
| Reference Key |
ewu2015frontierstwo
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|---|---|
| Authors | ;Jinzi eWu;Xiaoting eLuo;Xiaoting eLuo;Liang-Jun eYan |
| Journal | Journal of clinical and experimental dentistry |
| Year | 2015 |
| DOI |
10.3389/fphys.2015.00098
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| URL | |
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