Dear ALL:
What I am thinking to do is something like this. The protein is alkylated
with iodoacetamide-like and cut with CNBr before subjected to 2D
electrophoresis. I am not keen on such protein chemistry, wondering these
questions: Can I use TBP (tributyl phosphine) instead DTT for the reduction
step? Does TBP react with iodoacetamide? Do I have to get rid of these
reagents before doing CNBr cleavage? Does CNBr cleave at the newly formed
thioether site (cysteine)? I know CNBr clavage is quite specific, but I
havenot seen any 2D pictures of CNBr peptides. Can anybody tell me how they
perform?
Any responses to these questions are highly appreciated!
Thank you!
Guo-An
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