Hello,
I'm having some trouble with the solubilization of proteins contained
in a lipidic secretion we're studying (using 2DE).
To overcome this problem, I'm preparing a series of trials with
different lysis buffers, prepared with detergents
alternative/complementary to CHAPS.
One of the alternatives mentioned in the literature is Triton X-100,
but in some papers it appears that this detergent doesn't help
solubilize hydrophobic proteins but rather precipitates them, creating
a 2 fractions (hydrophilic and hydrophobic proteins). Is this true or
am I misinterpreting?
Any help will be very welcome.
Thank you,
Diana
