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Mitsugu Akagawa

Researcher at Osaka Prefecture University

Publications -  59
Citations -  2674

Mitsugu Akagawa is an academic researcher from Osaka Prefecture University. The author has contributed to research in topics: Oxidative deamination & Pyrroloquinoline quinone. The author has an hindex of 29, co-authored 59 publications receiving 2269 citations. Previous affiliations of Mitsugu Akagawa include Nagoya University & Tohoku University.

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Production of hydrogen peroxide by polyphenols and polyphenol-rich beverages under quasi-physiological conditions.

TL;DR: The features of the H2O2-generating property of green tea, black tea, and coffee were in good agreement with that of phenolic compounds, suggesting that polyphenols are responsible for the generation of H2 O2 in beverages.
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Covalent modification of proteins by green tea polyphenol (-)-epigallocatechin-3-gallate through autoxidation.

TL;DR: It is proposed that the covalent modification of proteins by EGCG may be a novel pathway related to the biological activity of EGC G, which has various beneficial properties including chemopreventive, anticarcinogenic, and antioxidant actions.
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Proteomic Analysis of Wheat Flour Allergens

TL;DR: A more detailed and comprehensive characterization of the wheat allergens involved in food allergy to wheat using proteomic strategies, referred to as "allergenomics", is achieved and nine subunits of LMW glutenins were identified as the most predominant IgE-binding antigens.
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Measurement of Glucose Uptake in Cultured Cells

TL;DR: In this article, a brief overview of glucose uptake assays in cultured cells is presented, including a method for measuring glucose uptake using radiolabeled 3-O-methylglucose.
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Human Serum Albumin as an Antioxidant in the Oxidation of ()-Epigallocatechin Gallate: Participation of Reversible Covalent Binding for Interaction and Stabilization

TL;DR: The results suggest the reversible covalent modification of EGCg via Schiff-base formation, and that the immobilization of E GCg to HSA, through the formation of a stable complex, prevented the polymerization and decomposition ofEGCg in human serum.