Dear All
There is a 43kd protein purified via Ni-chelating affinity
chromatography, anion exchange chromatography and gel filtration chromatography
in sequence. However the chromatogram obtained showed an extremely asymmetric
peak shape. The aggregation forms of proteins are mainly in the range of
monomers and dimers(Hepes and low concentration of salt were used as buffers
for gel filtration chromatography). 5% glycerinum and 1mM Benzamidine
hydrochloride had been added in order to maintain the stability of the protein
and prevent it from degrading. But well, all the efforts seem to be useless. We
wonder if there are any effective measures can be taken to radically solve this
problem. We would be much indebted for the suggestions you offer.
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