Verification of the universal versatility of a quantitative protein measurement technique using a metal mesh device

Seiji Kamba, Hirokazu Seto, Takashi Kondo, Yoshiko Miura

Research output: Contribution to journalArticle

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Abstract

When proteins are attached to microstructures such as a metal mesh device, changes in their optical properties occur. These changes have been characterized based on actual measurements in the infrared region of the spectrum. We have previously theoretically and experimentally demonstrated the optical changes associated with streptavidin. Here, we investigate three types of proteins: avidin, BSA, and lysozyme. The three proteins were adsorbed onto three types of metal mesh devices having different resonant frequencies, and the corresponding spectra were measured in the infrared region. The change in the frequency of the dip point in the spectrum was extracted to quantitatively determine the quantity of protein; these results were correlated with the quantitative measurements obtained by electrophoresis. By examining three types of different proteins, it was verified that a variety of proteins can be measured based on the optical characteristics of metal mesh devices.

Original languageEnglish
Pages (from-to)765-770
Number of pages6
Journalanalytical sciences
Volume34
Issue number7
DOIs
Publication statusPublished - Jan 1 2018

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Metals
Proteins
Infrared radiation
Streptavidin
Avidin
Muramidase
Electrophoresis
Natural frequencies
Optical properties
Microstructure

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry

Cite this

Verification of the universal versatility of a quantitative protein measurement technique using a metal mesh device. / Kamba, Seiji; Seto, Hirokazu; Kondo, Takashi; Miura, Yoshiko.

In: analytical sciences, Vol. 34, No. 7, 01.01.2018, p. 765-770.

Research output: Contribution to journalArticle

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