| Literature DB >> 26835606 |
Sarah Trimpin1, Shameemah Thawoos2, Casey D Foley2, Daniel W Woodall2, Jing Li2, Ellen D Inutan2, Paul M Stemmer3.
Abstract
Matrix-assisted ionization (MAI) is demonstrated to be a robust and sensitive analytical method capable of analyzing proteins such as cholera toxin B-subunit and pertussis toxin mutant from conditions containing relatively high amounts of inorganic salts, buffers, and preservatives without the need for prior sample clean-up or concentration. By circumventing some of the sample preparation steps, MAI simplifies and accelerates the analytical workflow for biological samples in complex media. The benefits of multiply charged ions characteristic of electrospray ionization (ESI) and the robustness of matrix-assisted laser desorption/ionization (MALDI) can be obtained from a single method, making it well suited for analysis of proteins and other biomolecules at ultra-high resolution as demonstrated on an Orbitrap Fusion where protein subunits were resolved for which MALDI-time-of-flight failed. MAI results are compared with those obtained with ESI, MALDI, and laserspray ionization methods and fundamental commonalities discussed.Entities:
Keywords: High resolution; Ionization; Laserspray; Mass spectrometry; Matrix-assisted; Protein
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Year: 2016 PMID: 26835606 PMCID: PMC4930895 DOI: 10.1016/j.ymeth.2016.01.019
Source DB: PubMed Journal: Methods ISSN: 1046-2023 Impact factor: 3.608