Purification of proteins in denaturants
satish at a.chem.upenn.edu
Fri Sep 20 15:16:51 EST 1996
In article <51mfla$2suk at news.doit.wisc.edu> klenchin at facstaff.wisc.edu (Dima Klenchin) writes:
>->and we have not found an
>->ion-exhange resin to which the protein will bind in these buffers,
>That's VERY strange. Every protein, intact ot denatured, will bind
>to either cation- or anion exchanger (or you have high salt composition
>from Ni step?). Playing with pH helps to modulate
>the strenght of binding.
Not in 4 M Guanidine HCL. Urea should work much better... you may want to
add 1 mM lysine to all the buffers so as to prevent carbamylation of
lysine residues by urea breakdown products.
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