By Topic

Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry Using a Mid-Infrared Tunable Laser for Direct Protein Analysis

Sign In

Cookies must be enabled to login.After enabling cookies , please use refresh or reload or ctrl+f5 on the browser for the login options.

Formats Non-Member Member
$31 $13
Learn how you can qualify for the best price for this item!
Become an IEEE Member or Subscribe to
IEEE Xplore for exclusive pricing!
close button

puzzle piece

IEEE membership options for an individual and IEEE Xplore subscriptions for an organization offer the most affordable access to essential journal articles, conference papers, standards, eBooks, and eLearning courses.

Learn more about:

IEEE membership

IEEE Xplore subscriptions

3 Author(s)

Matrix-assisted laser desorption/ionization (MALDI) using a mid-infrared (MIR) laser is a promising technique for the study of biomolecules. We achieved the measurement of an insoluble protein under strong denaturing conditions using two lasers, a UV laser and a free electron laser (FEL). The FEL is a powerful tool for the IR-MALDI; however, it is expensive and difficult to operate. We developed a MIR-MALDI time-of-flight mass spectrometer combined with a tunable MIR nanosecond pulsed laser, which was developed by the Institute of Physical and Chemical Research (RIKEN; Wako, Japan) and Kawasaki Heavy Industries, Ltd. (Tokyo, Japan). We evaluated the advantages of MIR-MALDI using this MIR nanosecond pulsed laser with a urea matrix and compared the results with that from previous study using the FEL. The molecular mass of insulin with urea was obtained at wavelength between 5.8 and 6.2 mum, which corresponds to the >C=O stretching vibration mode. In particular, a high SNR was observed at a wavelength of 5.9 mum. This technique produced a better SNR than that of a previous study that used the FEL.

Published in:

Selected Topics in Quantum Electronics, IEEE Journal of  (Volume:14 ,  Issue: 1 )