Ammonium sulfate and SDS (and more)
eoconNOeoSPAM at eez.csic.es.invalid
Thu Jul 27 14:01:03 EST 2000
I have some protein samples that were electroeluted
from a SDS-polyacrylamide gel, so they are with SDS and the
usual components of the gel and the running buffer. I want
to remove all these components as I want to perform a
digestion of these samples... I don't know how to broach
the matter. Could you help me?
I have considered the precipitation with acetone of
the protein, but I found really difficult the resuspension.
I later though on using any column to separate SDS
and proteins, but I had no good results.
I finally thought it could be a good idea to
precipitate proteins with ammonium sulfate, and later
remove the salt with a little Sephadex G-25 column. But
there are things I don't know. Will all SDS be in solution
if I precipitate the proteins like this? Or will the SDS
that is surrounding my protein remain like this, associated
to it, even having precipitated the protein? I found
nothing in the literature and I wanted to perform an
experiment to elucidate it, but I cannot find any method to
detect SDS easily (I cannot use the easiest method of
shaking and seeing if bubbles are formed, because the
concentred protein solutions are also aphrogen...). Could
you give me any idea?
Thank you in advance,
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