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Titolo:
Characterization of enzymes involved in biotransformation of polycyclic aromatic hydrocarbons in terrestrial isopods
Autore:
de Knecht, JA; Stroomberg, GJ; Tump, C; Helms, M; Verweij, RA; Commandeur, J; van Gestel, CAM; van Straalen, NM;
Indirizzi:
Vrije Univ Amsterdam, Inst Ecol Sci, Amsterdam, Netherlands Vrije Univ Amsterdam Amsterdam Netherlands Sci, Amsterdam, Netherlands Vrije Univ Amsterdam, Inst Environm Studies, Amsterdam, Netherlands Vrije Univ Amsterdam Amsterdam Netherlands dies, Amsterdam, Netherlands Vrije Univ Amsterdam, Dept Mol Toxicol, Amsterdam, Netherlands Vrije Univ Amsterdam Amsterdam Netherlands icol, Amsterdam, Netherlands
Titolo Testata:
ENVIRONMENTAL TOXICOLOGY AND CHEMISTRY
fascicolo: 7, volume: 20, anno: 2001,
pagine: 1457 - 1464
SICI:
0730-7268(200107)20:7<1457:COEIIB>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
FUNCTION OXIDASE ACTIVITY; GLUTATHIONE TRANSFERASES; MONOOXYGENASE SYSTEM; SULFATE CONJUGATIONS; HOMARUS-AMERICANUS; PORCELLIO SCABER; SPINY LOBSTER; HEPATOPANCREAS; CYTOCHROME-P450; BENZOPYRENE;
Keywords:
polycyclic aromatic hydrocarbons; mixed-function oxidases; glutathione-S-transferase; UDP-glucosyl-transferase; sulfotransferase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: de Knecht, JA Vrije Univ Amsterdam, Inst Ecol Sci, Amsterdam, Netherlands Vrije Univ Amsterdam Amsterdam Netherlands m, Netherlands
Citazione:
J.A. de Knecht et al., "Characterization of enzymes involved in biotransformation of polycyclic aromatic hydrocarbons in terrestrial isopods", ENV TOX CH, 20(7), 2001, pp. 1457-1464

Abstract

Little is known about the capacity of terrestrial invertebrates to transform organic soil pollutants such as polycyclic aromatic hydrocarbons (PAHs). Studies were designed to characterize microsomal mixed function oxygenase and accompanying conjugation enzymes from the hepatopancreas of the terrestrial isopods Porcellio scaber and Oniscus asellus using pyrene and hydroxypyrene as model substrates. The hydroxylation of pyrene and the formation ofpyreneglucoside and pyrenesulfate appeared to be sensitive measures for the activity of cytochrome P450 aryl hydrocarbon hydroxylase (AHH), uridinediphosphateglucosyl-transferase (UDPGT). and aryl sulfotransferase (ST), respectively. Treatment with the antibiotic riphampicine demonstrated that the enzyme activities originate from the animals themselves and not from symbiotic microflora present in the hepatopancreas and the gut. In both species. ST has a very high affinity for 1-hydroxypyrene with K-m values two orders of magnitude lower than that of UDPGT. The V-max values of UDPGT, however, are 10- to 20-fold higher than that of ST. Taking the P450 activities into consideration, both species are expected to transform PAHs in an equally effective way. When the isopods were fed with food containing benzo[a]pyrene and 3-methyl-cholanthrene, none of the enzyme activities appeared to be inducible except for a small enhancement of UDPGT in O. asellus. Our findings indicate that terrestrial isopods have a high, noninducible capacity for biotransformation of PAHs and that the sulfate conjugation pathway is as important as the carbohydrate conjugation pathway. This conclusion is consistent with the low body residues of parent PAHs found in the field.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 13:23:53