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The proteins were fractionated by three metal ions, Zn<jats:sup>2+<\/jats:sup>, Ni<jats:sup>2+<\/jats:sup> and Cu<jats:sup>2+<\/jats:sup>, immobilized on iminodiacetic acid and then separated by 2\u2010DE. The total number of protein spots resolved by 2\u2010DE increased approximately twofold when the proteins were prefractionated by IMAC. By establishing 2\u2010DE standard patterns, 371 proteins were selected and then characterized according to their specificity in binding the three different metal ions. Only 48 proteins did not bind to any of the three metal ions investigated. Cu<jats:sup>2+<\/jats:sup> was the most efficient ion in binding different proteins (310) compared to the other metals. Cu<jats:sup>2+<\/jats:sup> bound to 42 proteins specifically and to 268 proteins unspecifically. 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