Protein Ionization by Novel Mass Spectrometry Using Mid-Infrared Difference Frequency Generation Laser

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  • SATO Izuru
    Division of Sustainable Energy and Environmental Engineering, Graduate School of Engineering, Osaka University
  • YOSHIHASHI Sachiko
    Division of Sustainable Energy and Environmental Engineering, Graduate School of Engineering, Osaka University
  • SUZUKI Sachiko
    Division of Sustainable Energy and Environmental Engineering, Graduate School of Engineering, Osaka University
  • HAZAMA Hisanao
    Division of Sustainable Energy and Environmental Engineering, Graduate School of Engineering, Osaka University
  • AWAZU Kunio
    Division of Sustainable Energy and Environmental Engineering, Graduate School of Engineering, Osaka University

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Other Title
  • 中赤外波長可変固体レーザーを用いた新規質量分析装置によるタンパク質のイオン化
  • チュウ セキガイ ハチョウ カヘン コタイ レーザー オ モチイタ シンキ シツリョウ ブンセキ ソウチ ニ ヨル タンパクシツ ノ イオンカ

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Abstract

Matrix-assisted laser desorption/ionization (MALDI) is an important method to analyze such biomolecules as proteins. In particular, MALDI using an infrared laser (IR-MALDI) is expected to measure various samples such as sugar chains, lipids, and cells because a molecular vibration can be directly excited by IR laser. We developed an IR-MALDI time-of-flight mass spectrometer (TOFMS) using a tunable IR laser (Difference Frequency Generation laser: DFG laser) that can adjust wavelength from 5.5 to 10 μm. The mass-to-charge spectra of insulin with a succinic acid matrix can be taken at a wavelength of 5.8 μm, which differs from the infrared absorption of succinic acid. With a urea or sinapic acid matrix, insulin spectra are detected by irradiating the DFG laser with the wavelength shifted from the absorption of these matrices.

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