If your protein is so negatively charged why not use that and make a first
purification using an IEC?
<ruben_martherus at yahoo.com> wrote in message
news:20021213023520.1362.qmail at ww02.hostica.com...
> I've expressed a GST-fusion protein (original size ~24 kDa). The protein
is expressed and shows on SDS-PAGE a band of correct size. However my
purification of the protein (using Glutathione-Agarose beads, Sigma
according to manufacturer) is not working. I've tried things like, changing
buffers, pH, incubation time etc. The control (GST only) works ok, and also
another fusion protein has no problems. The protein fused to GST is highly
negatively charged at the pH at which the experiments are done. Does
somebody have any suggestions?
>> Thank you,
>> S.R.M. Martherus
>>>>http://biowww.net/mynews/tree.php?group_name=bionet_molbio_proteins&begin=0
