Record number :
2126454
Title of article :
Contamination of deconjugation enzymes derived from Helix pomatia with the plant bioactive compounds 3,3′-diindolylmethane, 5-methoxypsoralen, and 8-methoxypsoralen
Author/Authors :
Ainslie-Waldman، نويسنده , , Cheryl E. and Simpkins، نويسنده , , Scott W. and Upadhyaya، نويسنده , , Pramod and Carmella، نويسنده , , Steven G. and Hecht، نويسنده , , Stephen S. and Trudo، نويسنده , , Sabrina P. Ramet، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2013
Pages :
6
From page :
188
To page :
193
Abstract :
Bioactive compounds from plant foods are intensely investigated for effects on disease prevention. β-Glucuronidase/arylsulfatase from Helix pomatia (snail) is commonly used when quantifying exposure to metabolized dietary components. However, we describe here the contamination of multiple formulations of this enzyme preparation with 3,3′-diindolylmethane (DIM), 8-methoxypsoralen (8-MOP), and 5-methoxypsoralen (5-MOP), bioactives from cruciferous and apiaceous vegetables under investigation as putative cancer chemopreventive agents. We identified an Escherichia coli preparation of β-glucuronidase as free from contamination with any of the compounds tested. results demonstrate the importance of selecting appropriate enzyme preparations when quantifying naturally occurring, trace level compounds in biological fluids.
Keywords :
3?-Diindolylmethane , 5-Methoxypsoralen , Helix pomatia , Deconjugation enzymes , Dietary chemoprevention , 3 , 8-Methoxypsoralen
Journal title :
Food and Chemical Toxicology
Serial Year :
2013
Link To Document :
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