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Proceedings Paper

FT-IR analysis of phosphorylated protein
Author(s): Katsunori Ishii; Sachiko Suzuki Yoshihashi; Kunihiro Chihara; Kunio Awazu
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Paper Abstract

Phosphorylation and dephosphorylation, which are the most remarkable posttranslational modifications, are considered to be important chemical reactions that control the activation of proteins. We examine the phosphorylation analysis method by measuring the infrared absorption peak of phosphate group that observed at about 1070cm-1 (9.4μm) with Fourier Transform Infrared Spectrometer (FT-IR). This study indicates that it is possible to identify a phosphorylation by measuring the infrared absorption peak of phosphate group observed at about 1070 cm-1 with FT-IR method. As long as target peptides have the same amino acid sequence, it is possible to identify the phosphorylated sites (threonine, serine and tyrosine).

Paper Details

Date Published: 8 September 2004
PDF: 5 pages
Proc. SPIE 5461, Biophotonics New Frontier: From Genome to Proteome, (8 September 2004); doi: 10.1117/12.541092
Show Author Affiliations
Katsunori Ishii, Nara Institute of Science and Technology (Japan)
Osaka Univ. (Japan)
Sachiko Suzuki Yoshihashi, Osaka Univ. (Japan)
Kunihiro Chihara, Nara Institute of Science and Technology (Japan)
Kunio Awazu, Osaka Univ. (Japan)


Published in SPIE Proceedings Vol. 5461:
Biophotonics New Frontier: From Genome to Proteome
Michel D. Faupel; Patrick Meyrueis, Editor(s)

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