Abstract:
:The feasibility of an oxygen-independent mechanism of chloroform bioactivation was indicated by the covalent binding to lipid and protein occurring in anaerobic incubations of CHCl3 and microsomes in the presence of NADPH. Under these conditions, the loss of cytochrome P-450 and the inhibition of related monoxygenases were also observed. The chloroform anoxic biotransformation was negligible in uninduced microsomes and seemed to be catalyzed mainly by phenobarbital-inducible P-450 isozymes. Biotransformation could also be supported by NADH as the source of reducing equivalents. Anaerobic metabolism of chloroform led to decreased levels of the main PB-induced P-450 isozymes even at low CHCl3 concentration and did not affect benzo[a]pyrene hydroxylase activity. These effects were not decreased by thiolic compounds. The oxidation products of chloroform caused a general impairment of the monoxygenase system, probably related to the formation of protein aggregates with very high molecular weight. In the presence of physiological concentrations of GSH, the targets of aerobically-produced metabolites were lipids and, to a smaller extent, P-450. At low CHCl3 concentrations and/or in the presence of GSH the most changes to microsomal structures seemed to be produced by the reductively-formed intermediates.
journal_name
Chem Biol Interactjournal_title
Chemico-biological interactionsauthors
Testai E,Vittozzi Ldoi
10.1016/s0009-2797(86)80063-1subject
Has Abstractpub_date
1986-09-01 00:00:00pages
157-71issue
2eissn
0009-2797issn
1872-7786journal_volume
59pub_type
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journal_title:Chemico-biological interactions
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journal_title:Chemico-biological interactions
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journal_title:Chemico-biological interactions
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journal_title:Chemico-biological interactions
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journal_title:Chemico-biological interactions
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journal_title:Chemico-biological interactions
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