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Results clearly showed that the tyrosine-nitration level was reduced in proportion to the molar ratios of GSSSG and LASSS relative to HGF, as revealed by the decrease in anti-nitroY mAb-positive HGF (60-kDa -chain and 90-kDa proform) normalized to total HGF -chain as a loading control, that was monitored by stripping with SDS-ME solution and re-probing the blot with anti-HGF -chain N-terminal domain mAb (Figure 1b,c, second and third rows)

In summary, our results demonstrated that TG2 in cell lysates causes GST aggregate formation through crosslinking activity, which interferes with pulldown experiments and alters fused protein function