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Analysis of the multimeric state of proteins by matrix assisted laser desorption/ionization mass spectrometry after cross‐linking with glutaraldehyde
Author(s) -
Helin Jari,
Caldentey Javier,
Kalkkinen Nisse,
Bamford Dennis H.
Publication year - 1999
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/(sici)1097-0231(19990215)13:3<185::aid-rcm481>3.0.co;2-o
Subject(s) - chemistry , glutaraldehyde , mass spectrometry , matrix assisted laser desorption/ionization , chromatography , matrix (chemical analysis) , ionization , desorption , protein mass spectrometry , analytical chemistry (journal) , electrospray ionization , organic chemistry , ion , adsorption
We have undertaken a systematic study on the suitability of matrix‐assisted laser desorption/ionization mass spectrometry to analyze and determine the multimericity of several proteins after cross‐linking with glutaraldehyde. Using both commercially available proteins and others of viral origin currently being characterized in our laboratory, we studied the range of concentrations of cross‐linker and protein for optimal analysis. Under the conditions developed during this study, we confirmed the multimeric states of three phage PRD1 structural proteins with monomeric masses ranging from 13.5 to 63 kDa. In addition, we addressed the question of the general applicability of the method by using it successfully to confirm the stoichiometry of the heptameric chaperonin GroEL, a bacterial protein with a mass well over 450 kDa. Copyright © 1999 John Wiley & Sons, Ltd.