Young Researcher Paper Award 2023
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Print: ISSN 0914-4935
Online: ISSN 2435-0869
Sensors and Materials
is an international peer-reviewed open access journal to provide a forum for researchers working in multidisciplinary fields of sensing technology.
Online: ISSN 2435-0869
Sensors and Materials
is an international peer-reviewed open access journal to provide a forum for researchers working in multidisciplinary fields of sensing technology.
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Sensors and Materials
is covered by Science Citation Index Expanded (Clarivate Analytics), Scopus (Elsevier), and other databases.
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Sensors and Materials
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is covered by Science Citation Index Expanded (Clarivate Analytics), Scopus (Elsevier), and other databases.
Instructions to authors
English 日本語
Instructions for manuscript preparation
English 日本語
Template
English
Publisher
MYU K.K.
Sensors and Materials
1-23-3-303 Sendagi,
Bunkyo-ku, Tokyo 113-0022, Japan
Tel: 81-3-3827-8549
Fax: 81-3-3827-8547
MYU Research, a scientific publisher, seeks a native English-speaking proofreader with a scientific background. B.Sc. or higher degree is desirable. In-office position; work hours negotiable. Call 03-3827-8549 for further information.
MYU Research
(proofreading and recording)
MYU K.K.
(translation service)
The Art of Writing Scientific Papers
(How to write scientific papers)
(Japanese Only)
Sensors and Materials, Volume 36, Number 8(1) (2024)
Copyright(C) MYU K.K.
Copyright(C) MYU K.K.
|
pp. 3227-3238
S&M3729 Research Paper of Special Issue https://doi.org/10.18494/SAM4816 Published: August 2, 2024 Orthogonality of α-Sulfoquinovosidase in Human Cells and Development of Its Fluorescent Substrate [PDF] Ryosuke Yoshida, Ryosei Kaguma, Ryosuke Kaneko, Ichiro Matuso, Makoto Yoritate, Go Hirai, Takamasa Teramoto, Yoshimitsu Kakuta, Kosuke Minamihata, Noriho Kamiya, Teruki Nii, Akihiro Kishimura, Takeshi Mori, and Yoshiki Katayama (Received December 4, 2023; Accepted March 28, 2024) Keywords: enzyme, cell ELISA, fluorescence
Human orthogonal enzymes (HOEs), do not show the same activities as the endogenous enzymes of human cells and thus are useful as amplification enzymes to detect antigen proteins in biological samples. Here, we evaluates a new HOE from Escherichia coli, α-sulfoquinovosidase (α-SQase). We confirmed that the activity of α-SQase did not exist in examined human cell lines, and thus it was applicable to live-cell enzyme-linked immunosorbent assay (ELISA) in which the antigen membrane protein on cells was detected without inactivating endogenous enzymes, a pretreatment required for cell ELISA using conventional amplification enzymes. Here, we also developed a fluorescent substrate for α-SQase whose active residue is located at the end of the narrow, deep pocket of the substrate recognition site. The designed methylumbelliferyl substrate with a hydroxyl benzyl alcohol linker showed similar reactivity as the p-nitrophenol substrate, a good substrate for α-SQase.
Corresponding author: Takeshi Mori and Yoshiki Katayama  This work is licensed under a Creative Commons Attribution 4.0 International License. Cite this article Ryosuke Yoshida, Ryosei Kaguma, Ryosuke Kaneko, Ichiro Matuso, Makoto Yoritate, Go Hirai, Takamasa Teramoto, Yoshimitsu Kakuta, Kosuke Minamihata, Noriho Kamiya, Teruki Nii, Akihiro Kishimura, Takeshi Mori, and Yoshiki Katayama, Orthogonality of α-Sulfoquinovosidase in Human Cells and Development of Its Fluorescent Substrate, Sens. Mater., Vol. 36, No. 8, 2024, p. 3227-3238. |
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