Everything depends on the affinity of the metal for the enzyme. Also of importance is what type of co-factor. Some metals can be removed from some enzyme with chelating agents.
In the case of cytochrome c peroxidase people have used organic solvent at low pH to remove the heme co-factor.
Hope this helps
Marc
For weakly bound metal ions, adding a strong chelator like EDTA will remove them. For structural metal ions, it may be necessary to denature the enzyme in urea or guanidine, or with heat.
Dear Marc Ouellet and Adam Shapiro thanks for the reply. I am working on n-acetlytranferases, it has calcium ion as cofactor. I am interested in ellucidating the enzymatic activity in the absence of calcium ions. How should go about with this study?
Thanks
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