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 |
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Pages (from-to) | 1013-1015 |
Number of pages | 3 |
Journal | Chemosphere |
Volume | 76 |
Issue number | 7 |
DOIs | |
Publication status | Published - Aug 1 2009 |
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All Science Journal Classification (ASJC) codes
- Environmental Engineering
- Environmental Chemistry
- Chemistry(all)
- Pollution
- Health, Toxicology and Mutagenesis
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Metabolism of tributyltin and triphenyltin by Dall's porpoise hepatic microsomes. / Yang, Jian; Oshima, Yuji; Sei, Ito; Miyazaki, Nobuyuki.
In: Chemosphere, Vol. 76, No. 7, 01.08.2009, p. 1013-1015.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Metabolism of tributyltin and triphenyltin by Dall's porpoise hepatic microsomes
AU - Yang, Jian
AU - Oshima, Yuji
AU - Sei, Ito
AU - Miyazaki, Nobuyuki
PY - 2009/8/1
Y1 - 2009/8/1
N2 - 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.
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.
UR - http://www.scopus.com/inward/record.url?scp=67651115828&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=67651115828&partnerID=8YFLogxK
U2 - 10.1016/j.chemosphere.2009.05.010
DO - 10.1016/j.chemosphere.2009.05.010
M3 - Article
C2 - 19515398
AN - SCOPUS:67651115828
VL - 76
SP - 1013
EP - 1015
JO - Chemosphere
JF - Chemosphere
SN - 0045-6535
IS - 7
ER -