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©The Author(s) 2015.
World J Biol Chem. Nov 26, 2015; 6(4): 366-378
Published online Nov 26, 2015. doi: 10.4331/wjbc.v6.i4.366
Published online Nov 26, 2015. doi: 10.4331/wjbc.v6.i4.366
Figure 1 Glyceraldehyde 3-phosphate dehydrogenase isoforms in A549 cells.
A: 2D gel separation (pH range 3-11) of proteins from the nuclear (NE) and the cytosolic (CE) fraction of A549 cells after 1 μmol/L araC treatment for 24 h. The membrane was developed with anti-GAPDH antibody as described in “Materials and Methods”; B: Proteins from the cytosolic fraction were separated by 2D gel (pH range 6-11). Separated proteins were stained with SYPRO® Ruby (left panel), or developed with anti-GAPDH antibody (right panel). GAPDH: Glyceraldehyde 3-phosphate dehydrogenase; 2D: Two dimensional.
- Citation: Phadke M, Krynetskaia N, Mishra A, Barrero C, Merali S, Gothe SA, Krynetskiy E. Disruption of NAD+ binding site in glyceraldehyde 3-phosphate dehydrogenase affects its intranuclear interactions. World J Biol Chem 2015; 6(4): 366-378
- URL: https://www.wjgnet.com/1949-8454/full/v6/i4/366.htm
- DOI: https://dx.doi.org/10.4331/wjbc.v6.i4.366