Mutations in factor H reduce binding affinity to C3b and heparin and surface attachment to endothelial cells in hemolytic uremic syndrome
J. Clin. Invest. Tamara Manuelian, et al. 111:1181 doi:10.1172/JCI16651 [Go to this article.]

Figure 2
The mutant form of factor H binds less efficiently to heparin. Sera from a healthy control (a) and from HUS patient F106 with the R1210C mutation (b) were applied to heparin affinity chromatography, and after washing, bound proteins were eluted with the linear NaCl gradient. Individual fractions of 500 μl were collected starting at an NaCl concentration of 200 mM. The fractions were assayed by SDS-PAGE in combination with Western blotting. The 175-kDa mutant factor H eluted at a lower salt concentration (fraction 35) prior to the wild-type factor H protein (fraction 41). The arrow indicates the position of the mutant factor H protein.