Question

1) Is jumping from 50 mM NaCl to 500 mM NaCl an effective method for purification with anion exchange chromotrography? Why or why not?

2) Assuming that your protein was still impure following DEAE, what is a third type of purification technique that could be used to isolate the GFP?

3) Where would your protein be if you accidentally ran it down some Cation Exchange Resin?

Answer 1