Premium
Denaturation of metalloproteins with EDTA to facilitate enzymatic digestion and mass fingerprinting
Author(s) -
Janecki Dariusz J.,
Reilly James P.
Publication year - 2005
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1924
Subject(s) - chemistry , metalloprotein , ethylenediaminetetraacetic acid , mass spectrometry , matrix assisted laser desorption/ionization , digestion (alchemy) , chromatography , denaturation (fissile materials) , sample preparation in mass spectrometry , desorption , enzyme , biochemistry , chelation , electrospray ionization , inorganic chemistry , nuclear chemistry , organic chemistry , adsorption
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. Copyright © 2005 John Wiley & Sons, Ltd.