Identification of Proteins by Combination of MALDI-TOF Peptide Mass Fingerprinting and Fragmentation of Sulfonated Peptides

Authors

  • J. Lenco Department of Medical Biology and Genetics, Faculty of Medicine, Charles University, Hradec Kralove
  • J. Stulik Proteome Center for the Study of Intracellular Parasitism of Bacteria, Purkyne Military Medical Academy, Hradec Kralove,

Abstract

The MALDI TOF MS is an ideal method for routine identification of proteins separated by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). However, in some cases the outputs from peptide mass fingerprinting (PMF) do not enable unambiguous identification of proteins. In such situation, determination of a partial amino acid sequence of the target protein would be extremely helpful in the PMF identification. Sequencing using MALDI TOF post-source decay (PSD) usually generates complex spectra and the fragmentation is not complete. PSD sequencing with chemically assisted fragmentation allows to avoid these problems. Application of both methods in identification of proteins of Francisella tularensis is presented.

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Published

2004-06-15

How to Cite

Lenco, J., & Stulik, J. (2004). Identification of Proteins by Combination of MALDI-TOF Peptide Mass Fingerprinting and Fragmentation of Sulfonated Peptides. Chemické Listy, 98(5). Retrieved from http://ww-w.chemicke-listy.cz/ojs3/index.php/chemicke-listy/article/view/2141

Issue

Vol. 98 No. 5 (2004)

Section

Articles