Characterization of MATCH Chain Dimerization

Example 3

Efficient MATCH chain dimerization was further demonstrated by the remarkable homogeneity of the protein content in protein L-purified samples. The protein was analyzed over the course of four weeks and storage at 4° C. and 37° C. with respect to oligomerization by SE-HPLC and degradation by SDS-PAGE (see FIGS. 7 to 9). Prior to the study the sample concentration was adjusted to 1 g/L and t0 time points were determined. The monomer content was quantified by separation of the samples on a Shodex KW-402.5-4F (Showa Denko) and evaluation of the resulting chromatograms. For the calculation of the relative percentage of protein monomer the area of the monomeric peak was divided by the total area of peaks that could not be attributed to the sample matrix. The protein degradation was assessed by SDS-PAGE analysis with Any kD Mini-Protean TGX gels (Bio-Rad Laboratories) and stained with Coomassie brilliant blue. The protein concentration was monitored at the different time points by UV-Vis spectroscopy with an Infinity reader M200 Pro equipped with Nanoquant plate (Tecan Group Ltd.).