Figure 2.

Forms of immunoaffinity purified gelsolin. A and B shows 1DE analysis of gelsolin immunoaffinity purified from plasma and CSF respectively. A total of 15 μg immunoaffinity purified gelsolin was loaded per lane and gels were stained with Coommasie Brilliant Blue. Eight bands (labeled in lane A) were selected for mass spectrometric identification of proteins. A total of 2 μg recombinant gelsolin was used for analysis via Western blot; banding pattern differences were seen between goat anti-hGSN (lane C) and mouse anti-hGSN (lane D). The high molecular weight band - which is identified by an asterisk - was found to contain fibronectin, a protein known to bind gelsolin. All other bands contained gelsolin, which is further discussed in Table 1.