Denaturation of metalloproteins with EDTA to facilitate enzymatic digestion and mass fingerprinting.

Metal ions bound to a protein often stabilize tertiary and/or quaternary structure. Consequently, the digestion of metalloproteins that precedes analysis by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry is frequently incomplete. It is demonstrated that ethylenediaminetetraacetic acid (EDTA) successfully destabilizes metalloprotein structure and thereby facilitates tryptic digestion and protein identification.