Currently, I am working with a cibacron blue dye columne to purify a
dehydrogenase of my interest. The enzyme does not show activity without
NAD. As far as I know, cibacron blue has a relatively strong affinity
towards NAD requiring enzyme. To the contrary, the activity was found in
non-bound fractoin in my case. Can anyone give me a reasonable explanation
on this.
I'd also like to know the optimized elution strategy for this dye column
(although I know that it depends on the protein.).
Thanks.
Jang Lee,
jylee at boineer.kaist.ac.kr
