@article{ref1,
title="Acrolein detection based on alcohol dehydrogenase inhibition",
journal="International journal of environmental analytical chemistry",
year="2013",
author="Covaci, O.I. and Bucur, B. and Radu, G.L.",
volume="93",
number="3",
pages="325-334",
abstract="This paper presents the effect of acrolein on three dehydrogenases and proposes a fast spectrometric method for acrolein analysis. We have found that alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (AlDH) are inhibited by low acrolein concentrations (0.2 mM) while inhibition of glutamate dehydrogenase (GDH) is not observed even at higher acrolein concentrations (1 mM). Acrolein is a suicide substrate for AlDH and ADH inhibition by acrolein is competitive. Cysteine (L-Cys) and glutathione (GSH) react with acrolein and thus reduce its expected inhibitory effect. ADH was chosen to develop a spectrophotometric method for acrolein analysis based on enzyme inhibition. The calibration curve is linear between 0.2 and 1.0 mM acrolein. © 2013 Copyright Taylor and Francis Group, LLC.<p /><p>Language: en</p>",
language="en",
issn="0306-7319",
doi="10.1080/03067319.2011.581374",
url="http://dx.doi.org/10.1080/03067319.2011.581374"
}