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. Author manuscript; available in PMC: 2014 Jun 24.
Published in final edited form as: Protein Expr Purif. 2010 Dec 10;76(2):254–263. doi: 10.1016/j.pep.2010.12.002

Figure 3.

Figure 3

Validation of rFH by mass spectrometry and dynamic light scattering. (A) The candidate recombinant FH (peaks a and c correspond to double-charged and single-charged species, respectively) and an internal standard (IgG1; peaks b and d correspond to double-charged and single-charged species, respectively) were analysed on a MALDI-ToF mass spectrometer. The experimentally derived mass of ~138,000 Da is in good agreement with the theoretical mass of rFH. (B) Dynamic light scattering was performed on rFH in PBS at a concentration of 1 mg/ml. No indication of aggregation was observed.