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

Janecki Dariusz J. | Zendy; Reilly James P. | Zendy

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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.

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