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Efficient enrichment and desalting of protein digests using magnetic mesocellular carbon foams in matrix‐assisted laser desorption/ionization mass spectrometry
Author(s) -
Kim YoungPil,
Cho Kun,
Lee Dohoon,
Piao Yunxian,
Ahn Yeong Hee,
Yoo Jong Shin,
Hyun Taeghwan,
Kim HakSung
Publication year - 2007
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.3231
Subject(s) - chemistry , mass spectrometry , chromatography , matrix assisted laser desorption/ionization , desorption , protein mass spectrometry , adsorption , matrix (chemical analysis) , elution , ionization , analytical chemistry (journal) , tandem mass spectrometry , ion , organic chemistry
We demonstrate that magnetic mesocellular carbon foams (Mag‐MCF‐C) can be effectively used for enrichment and desalting of protein digests or peptides in matrix‐assisted laser desorption/ionization mass spectrometry (MALDI‐MS). The large mesocellular pores and surface area of Mag‐MCF‐C are likely to mainly contribute to high efficiency in enrichment and desalting of protein digests. The magnetic property of Mag‐MCF‐C enabled easy and simple enrichment and desalting process comprising adsorption, washing, and separation steps by using an external magnet. Following elution from Mag‐MCF‐C by using a matrix solution (CHCA in 70% ACN/0.1% TFA), the peptides were subjected to MALDI‐MS analysis. As a result, MALDI mass spectra of peptides or tryptic protein digests were distinct even at a peptide concentration as low as 50 pM. The use of Mag‐MCF‐C resulted in significantly improved sequence coverage for protein identification when compared to other conventional methods. Mag‐MCF‐C will find applications in mass spectrometric analysis of low abundance peptides or protein digests with high sensitivity. Copyright © 2007 John Wiley & Sons, Ltd.