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. 2014 Aug 19;9(8):e105409. doi: 10.1371/journal.pone.0105409

Figure 2. PSG2-immunoaffinity column purification of tyrosine-sulfated proteins from cow RPE.

Figure 2

(A). The elution profile was monitored by following absorbance at 280 nm. Following loading, the column was washed with buffers W1, W2, and W3. Elution was performed in buffer W3 containing 4 mM sulfated pentapeptide (EB). (B). Twenty-six microliter aliquots from input (IN), flow-through (FT), wash 1 (W1), and wash 2 (W2) were fractionated by SDS-PAGE, and proteins were visualized by staining with Coomassie blue dye. (C). Left, SDS-PAGE of 26 µL of wash 3 (W3) and eluted samples (EB) from the immunoaffinity column stained with Coomassie blue (CB) and right, immunoblotted with PSG2. Asterisks indicate the bands that were prominent on Coomassie blue-stained gel (CB) and were also recognized by PSG2 as tyrosine-sulfated.