I cleave my protein from its vector using Ni sulfate under high temperature and PH, after lyophilizing. My protein came out yellowish, and it should be white, so I assumed that there are some traces of Ni hydroxyde that might have been made under the harsh basic cleaving conditions. Now, I want to get rid of it, or even prove my theory. So I'm looking for a way to detect Ni hydroxyde, or to remove it from the sample.
You can easily test for Ni2+ with dimethylglyoxime (they should have it any undergrad inorganic lab) but I doubt it is Ni hydroxide since it is greenish as far as I remember.
EDTA will bind up any free Ni2+. However, I wonder what condition your protein must be in after treatment with high temperature and pH.
I actually add EDTA after the reaction then dialyse itl, and finally lyophilyze it
You can also try Ni-NTA agarose. You have to strip the nickel away first and then mix the NTA agarose with your sample. If it works you do not need dialysis.
See f.i.
http://www.piercenet.com/product/hispur-ni-nta-superflow-agarose
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