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 ethylenediaminet...

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Veröffentlicht in:	Rapid communications in mass spectrometry 2005-01, Vol.19 (10), p.1268-1272
Hauptverfasser:	Janecki, Dariusz J., Reilly, James P.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Carbonic Anhydrase II - chemistry Carbonic Anhydrase II - metabolism Carboxypeptidases A - chemistry Carboxypeptidases A - metabolism Cattle Edetic Acid - chemistry Edetic Acid - pharmacology Metalloproteins - chemistry Metalloproteins - metabolism Models, Molecular Molecular Weight Peptide Mapping - methods Protein Denaturation - drug effects Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Superoxide Dismutase - chemistry Superoxide Dismutase - metabolism Temperature Trypsin - metabolism
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Beschreibung
Zusammenfassung:	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.
ISSN:	0951-4198 1097-0231
DOI:	10.1002/rcm.1924