Covalent binding of benzo[a]pyrene to rat liver cytosolic proteins and its effect on the binding to microsomal proteins.

Abstract:

:Benzo[a]pyrene will bind covalently to rat liver cytosolic proteins when incubated with microsomes and NADPH. The binding is most extensive when microsomes from 3-methylcholanthrene-treated rather than phenobarbital-treated or control rats are used. The binding to cytosolic proteins increases when incubations are performed with increasing concentrations of cytosol. At the same time the covalent binding of benzo[a]pyrene to microsomal proteins decreases. Two cytosolic polypeptides are the main targets for benzo[a]pyrene. These have the same mobility in polyacrylamide gels as the subunits of purified glutathione S-transferase B. These subunits also react covalently with benzo[a]pyrene when the transferase is incubated with microsomes and NADPH.

journal_name

Biochem Pharmacol

journal_title

Biochemical pharmacology

authors

Schelin C,Tunek A,Jergil B

doi

10.1016/0006-2952(83)90472-0

subject

Has Abstract

pub_date

1983-05-01 00:00:00

pages

1501-6

issue

9

eissn

0006-2952

issn

1873-2968

pii

0006-2952(83)90472-0

journal_volume

32

pub_type

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