JMSSJ On-line, Vol. 51 (2003) No. 5, pp. 554-558
Modification of Cysteine Residue in Peptides by a Fluorescent Reagent for Complete Sequence Analyses Using Post-Source Decay Method in Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry
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    Masatoshi NAKAGAWA,a) Tohru YAMAGAKI b), and Hiroshi NAKANISHI *a)

    *a) Biological Information Research Center, National Institute of Advanced Industrial Science and Technology (Tsukuba Central 6, 1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan) b) Department of Chemistry, School of Science, The University of Tokyo (7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan)
In the sequence analyses of antigen peptides from nucleoprotein in influenza virus, it was very difficult to obtain the sufficient numbers of product ions using the post-source decay (PSD) method in MALDI-TOF-MS. Fluorescent modification of the thiol group of the cysteine residue in the target peptides using 5-iodoacetamide fluorescein was introduced for the PSD measurement. The fluorescently-labeled peptides gave sufficient product ions for complete sequence analyses in the PSD spectrum, which leads to the complete sequence analyses of the peptides with cysteine residue.
Key words: MALDI-TOF-MS, PSD method, Peptide sequence, Fluorescently modification, Nucleoprotein in influenza virus
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