Laboratory of Protein Profiling and Functional Proteomics


Toshifumi TAKAO

Chemical Biology


Institute for Protein Research



Research Theme

Mass spectrometry is well accepted technique for the analyses of chemical structures of biological compounds. 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 also apply the developed methods to structural analysis of micro quantities of peptides, proteins, and their related substances.

Development of chemical/analytical methods and software for analysis of protein primary structure by mass spectrometry

Recently, the chemical method for selective isolation of N-blocked peptides has been developed (Mikami & Takao, Anal. Chem. 2007). A novel polyacrylamide gel-based method has been developed for the affinity capture of specific proteins from a complex mixture (Awada et al. Anall.Chem. 2010).

Mass spectrometric analysis of post-translational modifications

Several novel post-translational modifications were elucidated by mass spectrometry: farnesylation at the C-terminal Cys, heterogeneous fatty acid modifications at the N-terminal Gly, ε-(γ-glutamyl)lysine in core histones, C-terminal lipidation by PE (Fig. 1), unsaturated fatty acid modification (Fig. 2), etc.

0Ubiquitination-like system mediates novel protein-lipidation. Nature, 408, 488 –492 (2000)

1Novel fatty acid modification (palmitoleoyl modification at Ser209) of Wnt protein essential for Wnt secretion (Takada R. et al. Developmental Cell, 11, 791-801 , 2006).


Awada, C. et al. Affinity-Trap Polyacrylamide Gel Electrophoresis: A Novel Method of Capturing Specific Proteins by Electro-Transfer Anal. Chem. 82 , 755 - 761 (2010)


Institute for Protein Research
Osaka Univeristy
TEL: 06-6879-4312, FAX: 06-6879-4332