Sequencing of argentinated peptides by means of matrix-assisted laser desorption/ionization tandem mass spectrometry
Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review
Author(s)
Detail(s)
Original language | English |
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Pages (from-to) | 2072-2082 |
Journal / Publication | Analytical Chemistry |
Volume | 74 |
Issue number | 9 |
Publication status | Published - 1 May 2002 |
Link(s)
Abstract
Argentinated peptide ions are formed in abundance under matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) conditions in the presence of Ag+ ions. These argentinated peptide ions are fragmented facilely under MALDI-MS/MS conditions to yield [bn + OH + Ag]+, [bn - H + Ag]+ and [an - H + Ag]+ ions that are indicative of the C-terminal sequence. These observations parallel those made earlier under electrospray MS conditions (Chu, I. K.; Guo, X.; Lau, T.-C.; Siu, K. W. M. Anal. Chem. 1999, 71, 2364-2372). A mixed protonated and argentinated tryptic peptide map was generated from 37 fmol of bovine serum albumin (BSA) using MALDI-MS. MALDI-MS/MS data from four argentinated peptides at a protein amount of 350 fmol unambiguously identified the protein as BSA. Sequence-tag analysis of two argentinated tryptic peptides was used to identify unambiguously myocyte enhancer factor 2A, which had been recombinantly expressed in a bacterial cell line.
Citation Format(s)
Sequencing of argentinated peptides by means of matrix-assisted laser desorption/ionization tandem mass spectrometry. / Chu, Ivan K.; Cox, David M.; Guo, Xu et al.
In: Analytical Chemistry, Vol. 74, No. 9, 01.05.2002, p. 2072-2082.
In: Analytical Chemistry, Vol. 74, No. 9, 01.05.2002, p. 2072-2082.
Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review