Sequencing of argentinated peptides by means of matrix-assisted laser desorption/ionization tandem mass spectrometry

Anal Chem. 2002 May 1;74(9):2072-82. doi: 10.1021/ac0111006.


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 [b(n) + OH + Ag]+, [b(n) - H + Ag]+ and [a(n) - 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • DNA-Binding Proteins / analysis
  • MEF2 Transcription Factors
  • Myogenic Regulatory Factors
  • Peptide Fragments / analysis*
  • Proteins / analysis
  • Sensitivity and Specificity
  • Sequence Analysis, Protein / instrumentation
  • Sequence Analysis, Protein / methods*
  • Serum Albumin, Bovine / analysis
  • Serum Albumin, Bovine / metabolism
  • Silver / chemistry*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods*
  • Transcription Factors / analysis
  • Trypsin / metabolism


  • DNA-Binding Proteins
  • MEF2 Transcription Factors
  • Myogenic Regulatory Factors
  • Peptide Fragments
  • Proteins
  • Transcription Factors
  • Serum Albumin, Bovine
  • Silver
  • Trypsin