In article <2q6job$21t at news.iastate.edu> bipin at iastate.edu (Bipin K Dalmia) writes:
>i'm trying to purify a protein expressed in e. coli. there is tons of it
>in the soluble extract. the pI is about 9.5. so naturally i tried using
>a cation exchanger at pH 6.5 but my protein flows right thru it. i've
>checked the ionic strengths etc. and they look good. the resin was
>properly equilibrated too. i'm using bio-rad's biorex-70 resin in the
>sodium form and eluting with a gradient of NaCl.
I wouldn't worry about it just yet, proteins don't have to bind just because
they have the opposite charge to the column, the charged might be in a hollow
or spread evenly over the surface. Go finf something that it will bind to.
Joe Mack
mack at ncifcrf.gov
>>any clues?
>>bip
>--
>bipin k. dalmia the other night i was lying on my bed, looking
>bipin at iastate.edu up at the beautiful stars, and i said to myself,
>n2.bkd at isumvs.iastate.edu 'where the F*CK is my ROOF !!'
>--
