Recently purified an unknown protein with a partial N-terminal
sequence match to a bacterial outermembrane protein. Oddly this
protein does not react with DTNB, does not seem to ionize when mixed
with sinnapinic acid and placed in a MALDI-ToF, and has a molecular
weight of 33kDa as judged by SDS PAGE analysis.
Curious to know if anybody thinks that membrane proteins would have
more difficulty interacting with MALDI matrices than other proteins?
