Laboratory of Protein Profiling and Functional Proteomics


Director Toshifumi TAKAO



Tel 81-6-6879-4312
Fax 81-6-6879-4312


Mass spectrometry is a well accepted technique for peptide sequencing and analysis of post-translational modification. In conjunction with accumulating protein and gene sequence databases, we are using state-of-the-art mass spectrometry for large-scale protein identification which is indispensable for proteomics research. We apply the following developed methods to the structural analysis of micro quantities of peptides, proteins, and their related substances.

Fig. 1: Novel fatty acid modification (palmitoleoyl modification at Ser209) of Wnt protein essential for Wnt secretion (Takada R. et al. Developmental Cell, 11, 791-801, 2006).
Fig.2 : Automated quantitation of a peptide by a WEB application, Isotopica ( An 18O-stable-isotope-labeled synthetic peptide was spiked into a urinary sample, and the resultant mixture was measured by MALDI-MS. (Rapid Commun. Mass Spectrom. 18, 2465, 2004; Nucleic Acids Res. 32, 674, 2004)

Current Research Programs

  1. Development of chemical/analytical methods and software for analysis of protein primary structure by mass spectrometry
  2. Mass spectrometric analysis of post-translational modifications
  3. Development of chemical and analytical methods for proteomics
  4. Study on fragmentation in mass spectrometry of peptides and carbohydrates
  5. Development of a chemical derivatization method (4-aminobenzoic acid 2-(diethylamino)ethyl ester) for high sensitive detection of sugar chains of a glycoprotein
  6. Hardware development for high-sensitivity mass spectrometry