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| I am working with a MBP-fusion protein. I need to rebind the purified protein to the amylose resin and need to remove maltose from my sample for that. My protein is very positive (pI 9.1) so i tried an ion exchange column with SP sepharose. It looks like that my protein precipitates on the column. Also the binding to the resin is low (40%). I also tried to run a gel filtration on the sample. But is it possible to remove the all the maltose "bound and unbound" using size exclusion? |
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| maltose , maltose removal , mbpfusion , removal , sec |
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