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Contamination of Deconjugation Enzymes Derived From Helix Pomatia With the Plant Bioactive Compounds 3,3'-diindolylmethane, 5-methoxypsoralen, and 8-methoxypsoralen

Contamination of Deconjugation Enzymes Derived From Helix Pomatia With the Plant Bioactive Compounds 3,3'-diindolylmethane, 5-methoxypsoralen, and 8-methoxypsoralen

Cheryl E Ainslie-Waldman, Scott W Simpkins, Pramod Upadhyaya, Steven G Carmella, Stephen S Hecht, Sabrina P Trudo

Food Chem Toxicol. 2013 Dec;62:188-93.

PMID: 23994708

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. These results demonstrate the importance of selecting appropriate enzyme preparations when quantifying naturally occurring, trace level compounds in biological fluids.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9001450-B	β-Glucuronidase from Helix pomatia		9001-45-0	Price
AP9016175	Sulfatase from Helix pomatia		9016-17-5	Price

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