Metabolism of tributyltin and triphenyltin by Dall's porpoise hepatic microsomes

Jian Yang; Yuji Oshima; Ito Sei; Nobuyuki Miyazaki

doi:10.1016/j.chemosphere.2009.05.010

Metabolism of tributyltin and triphenyltin by Dall's porpoise hepatic microsomes

Jian Yang, Yuji Oshima, Ito Sei, Nobuyuki Miyazaki

Animal and Marine Bioresource Sciences

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

Abstract

The in vitro metabolism of tributyltin (TBT) and triphenyltin (TPT) by the hepatic microsomal cytochrome P-450 system enzymes of Dall's porpoises (Phocoenoides dalli) was comparatively elucidated with those enzymes of the Sprague Dawley rat in the present study. Our results suggested firstly a limited metabolic capacity for TBT and especially TPT to their metabolites in the Dall's porpoises, and documented a similar mechanism of a relatively stronger metabolic rate of TBT to its metabolites than that of TPT in the microsome of porpoises and rat. However, the metabolic capacity to degrade both TBT and TPT were much lower in the microsome of porpoises than that in the rats.

Original language	English
Pages (from-to)	1013-1015
Number of pages	3
Journal	Chemosphere
Volume	76
Issue number	7
DOIs	https://doi.org/10.1016/j.chemosphere.2009.05.010
Publication status	Published - Aug 2009

All Science Journal Classification (ASJC) codes

Environmental Engineering
Environmental Chemistry
Chemistry(all)
Pollution
Health, Toxicology and Mutagenesis

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abstract = "The in vitro metabolism of tributyltin (TBT) and triphenyltin (TPT) by the hepatic microsomal cytochrome P-450 system enzymes of Dall's porpoises (Phocoenoides dalli) was comparatively elucidated with those enzymes of the Sprague Dawley rat in the present study. Our results suggested firstly a limited metabolic capacity for TBT and especially TPT to their metabolites in the Dall's porpoises, and documented a similar mechanism of a relatively stronger metabolic rate of TBT to its metabolites than that of TPT in the microsome of porpoises and rat. However, the metabolic capacity to degrade both TBT and TPT were much lower in the microsome of porpoises than that in the rats.",

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AU - Yang, Jian

AU - Oshima, Yuji

AU - Sei, Ito

AU - Miyazaki, Nobuyuki

PY - 2009/8

Y1 - 2009/8

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AB - The in vitro metabolism of tributyltin (TBT) and triphenyltin (TPT) by the hepatic microsomal cytochrome P-450 system enzymes of Dall's porpoises (Phocoenoides dalli) was comparatively elucidated with those enzymes of the Sprague Dawley rat in the present study. Our results suggested firstly a limited metabolic capacity for TBT and especially TPT to their metabolites in the Dall's porpoises, and documented a similar mechanism of a relatively stronger metabolic rate of TBT to its metabolites than that of TPT in the microsome of porpoises and rat. However, the metabolic capacity to degrade both TBT and TPT were much lower in the microsome of porpoises than that in the rats.

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Metabolism of tributyltin and triphenyltin by Dall's porpoise hepatic microsomes

Abstract

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