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. Author manuscript; available in PMC: 2015 Nov 5.
Published in final edited form as: J Neurochem. 2008 Feb 7;105(5):1979–1995. doi: 10.1111/j.1471-4159.2008.05288.x

Fig. 3.

Fig. 3

SDS-PAGE gels of DNA affinity purification fractions. Proteins from the indicated chromatographic fractions were resolved on an 11% SDS-PAGE gel and visualized by staining with Coomassie Blue. The gel in panel A contained a total of 5 µg of nuclear proteins per lane, while the gel in panel B contained only 3 µg/lane. The gels were placed on a clean plastic plate, and individual lanes cut sequentially into (3-mm) gel slices across their entire length. Proteins within the gel slices were digested (in-gel) with trypsin and the eluted peptides analyzed by mass spectrometry.