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Measurement of glyoxalase activities

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Arai, Makoto, Nihonmatsu‑Kikuchi, Naomi, Itokawa, Masanari, Rabbani, Naila and Thornalley, Paul J. (2014) Measurement of glyoxalase activities. Biochemical Society Transactions, 42 (2). pp. 491-494. 491. doi:10.1042/BST20140010 ISSN 0300-5127.

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Official URL: http://dx.doi.org/10.1042/BST20140010

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Abstract

Glyoxalase I catalyses the isomerization of the hemithioacetal formed non-enzymatically from methylglyoxal and glutathione to S-D-lactoylglutathione. The activity of glyoxalase I is conventionally measured spectrophotometrically by following the increase in A240 for which the change in molar absorption coefficient Δε240=2.86 mM⁻¹·cm⁻¹. The hemithioacetal is pre-formed in situ by incubation of methylglyoxal and glutathione in 50 mM sodium phosphate buffer (pH 6.6) at 37°C for 10 min. The cell extract is then added, the A240 is monitored over 5 min, and the initial rate of increase in A240 and hence glyoxalase I activity deduced with correction for blank. Glyoxalase I activity is given in units per mg of protein or cell number where one unit is the amount of enzyme that catalyses the formation of 1 μmol of S-D-lactoylglutathione per min under assay conditions. Glyoxalase II catalyses the hydrolysis of S-D-lactoylglutathione to D-lactate and glutathione. Glyoxalase II activity is also measured spectrophotometrically by following the decrease in A240 for which the change in molar absorption coefficient Δε240=-3.10 mM⁻¹·cm⁻¹. It is given in units per mg of protein or cell number where one unit is the amount of enzyme that catalyses the hydrolysis of 1 μmol of S-D-lactoylglutathione per min under assay conditions. Glyoxalase I and glyoxalase II activity measurements have been modified for use with a UV-transparent microplate for higher sample throughput.

Item Type: Journal Article
Subjects: Q Science > QR Microbiology
Divisions: Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Health Sciences
Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH): Glyoxalase, Gene expression
Journal or Publication Title: Biochemical Society Transactions
Publisher: Portland Press Ltd.
ISSN: 0300-5127
Official Date: 1 April 2014
Dates:
DateEvent
1 April 2014Published
7 January 2014Submitted
Volume: 42
Number: 2
Number of Pages: 4
Page Range: pp. 491-494
Article Number: 491
DOI: 10.1042/BST20140010
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Funder: Nihon Gakujutsu Shinkōkai [Japan Society for the Promotion of Science] (NGS)

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