Despite the importance of metal cofactors, techniques to measure metal status in a proteomic fashion are not readily available. One major challenge for metalloproteomics is determining the identity of the metalloprotein. Thus, we have been pursuing the development of tools that will allow the direct identification and quantitation of individual metalloproteins from biological samples.  The tools we have developed allow for comparative metalloproteomics and provide a metalloprotein map that is reminiscent of 2D polyacrylamide gels. The ability to resolve and measure metalloenzymes in detail have practical implications for a variety of research areas including neurodegeneration, cancer, aging, heavy metal toxicity and therapeutic development.  Here we present metalloprotein maps for Cu, Fe, Zn, Mn, Co, Ni and P from human brain tissue. The combination of multidimensional chromatography and traditional proteomics has provided one of the first in-depth looks at the human metallproteome and has resulted in the discovery of novel metalloproteins. The future development and application of this technique promises to yield important insights into the role of metals in biological and pathological processes.