zeru at zedat.fu-berlin.de
Sat Jun 6 03:20:00 EST 1998
I'm trying to purify a DNA-binding protein. After ion exchange
chromatography I'm using Dynabeads as the last purification step. The
DNA-binding activity is clearly detectable in the eluate (EMSAs). My
problem is that there is no band detectable in protein gels
I heard that it is possible to test samples with low protein quantity
with the method of mass spectroscopy, but the opinions seem to differ.
Someone said it's senseless, if I can't detect a band with
silverstaining. In this newsgroup I read that it's possible to sequence
quantities from femtomolar to picomolar quantities.
Since I have no idea about the method I would greatly appreciate any
comments. Which quantities can be measured? Is it possible to find out
how many different proteins are in the eluate?
Thank you very much in advance!
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