I imagine it will depend upon how your protein interacts with cadmium. If the metal is deeply buried in the protein, the affinity chromatography probably will not work because the metal is chelated by the resin and not sufficiently accessible. But if the protein binds the cadmium superficially, and can do so with only partial coordination, then it might work. Of course, the assumption is that the protein binds cadmium as an ion, not in the zero oxidation state, since the resin only binds the ion.
I imagine it will depend upon how your protein interacts with cadmium. If the metal is deeply buried in the protein, the affinity chromatography probably will not work because the metal is chelated by the resin and not sufficiently accessible. But if the protein binds the cadmium superficially, and can do so with only partial coordination, then it might work. Of course, the assumption is that the protein binds cadmium as an ion, not in the zero oxidation state, since the resin only binds the ion.
@Adam B shapiro thank you so much. So would you suggest if I apply tag e.g his tag etc?
Dear Asmara,
the answer from Adam says nearly all. We don't have experience with cadmium, but coupling onto NTA Agarose, as example from our company
https://cube-biotech.com/products/purification-resins/his-affinity-resins/nta-agarose-100/365/purecube-100-nta-agarose
works very well, when loaded with the homologue zinc and applying at zinc finger proteins and other zinc-interacting proteins. So, as the materials are inexpensive and metal loading is simple, it is worth a try, testing the material above (or, for sure, a cometitor material).
Apart from whether this works you should also consider the toxicity of Cd, that makes disposal of wastes expensive and complicated. Cd2+ can usually be replaced by less obnoxious ions, like Zn2+.
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