Metabolism-dependent binding of the chlorinated insecticide DDT and its metabolite, DDD, to microsomal protein and lipids.

Abstract:

:Dichlorodi[U-14C]phenyltrichloroethane ( [14C]DDT), incubated with rat hepatic microsomes and NADPH, produced reactive intermediates which covalently bound to microsomal protein and lipids. In atmospheric oxygen, DDT bound to microsomal protein; however, binding was increased up to approximately 70% by oxygen depletion. Low levels of [14C]DDT binding to microsomal lipids occurred under atmospheric oxygen but, in contrast to protein binding, DDT-phospholipid binding was increased up to 20-fold by oxygen depletion. Dichlorodiphenyldichloroethane (DDD) was rapidly formed from DDT under anaerobic conditions, although when DDD was utilized as substrate, binding to microsomal protein occurred only in the presence of oxygen. Sodium dithionite, added to microsomes, produced [14C]DDT phospholipid and protein binding, and DDD formation, but failed to support DDD metabolism or binding. The data are consistent with the reductive formation of a DDT free-radical intermediate that led to the formation of DDD and that was bound preferentially to microsomal lipids.

journal_name

Biochem Pharmacol

journal_title

Biochemical pharmacology

authors

Baker MT,Van Dyke RA

doi

10.1016/0006-2952(84)90483-0

subject

Has Abstract

pub_date

1984-01-15 00:00:00

pages

255-60

issue

2

eissn

0006-2952

issn

1873-2968

pii

0006-2952(84)90483-0

journal_volume

33

pub_type

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