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Increase in the Protein-Bound Form of Glutathione in Human Blood after the Oral Administration of Glutathione

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† Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Kyoto Prefectural University, 1-5 Hangi-cho, Shimogamo, Sakyo-ku, Kyoto 606-8522, Japan
‡ KOHJIN Life Sciences Company, Ltd., 1-3 Yurakucho 1-chome, Chiyoda-ku, Tokyo 100-0006, Japan
*(K.S.) Mail (present address): Division of Applied Biosciences, Graduate School of Agriculture, Kyoto University, Kitashirakawa Oiwake-cho, Kyoto 606-8502, Japan. Phone: +81-75-753-6444. Fax: +81-75-723-3503. E-mail: [email protected]
Cite this: J. Agric. Food Chem. 2014, 62, 26, 6183–6189
Publication Date (Web):May 30, 2014
https://doi.org/10.1021/jf501338z
Copyright © 2014 American Chemical Society
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    Abstract

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    The present study examined the impact of the supplementation of glutathione (GSH), γ-l-glutamyl-l-cysteinyl-glycine, on human blood GSH levels. Healthy human volunteers were orally supplemented with GSH (50 mg/kg body weight). Venous blood was collected from the cubital vein before and after ingestion. Plasma was mixed with 3 volumes of ethanol. The supernatant and precipitate were used for the deproteinized and protein fractions of plasma, respectively. Blood cell and plasma fractions were pretreated with 5% trichloroacetic acid–2% 2-mercaptoethanol to reduce the oxidized form of GSH and liberate protein-bound GSH. The 2-mercaptoethanol-pretreated GSH was determined by precolumn derivatization with 6-aminoquinolyl-N-hydroxy succinimidyl carbamate and liquid chromatography–tandem mass spectrometry. There was no significant difference in GSH contents in the deproteinized fraction of plasma and blood cell fraction after GSH ingestion. However, the GSH contents in the protein-bound fraction of plasma significantly (P < 0.01) increased from 60 to 120 min after GSH supplementation.

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