ISSN:
1432-1246
Keywords:
Trichloroethylene
;
Vinyl chloride
;
Rat liver microsomes
;
Covalent protein binding of trichloroethylene
;
Albumin
;
Lecithin liposomes
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Summary Microsomal uptake irreversible protein binding of labelled trichloroethylene was measured following incubation with rat liver microsomes in an all-glass vacuum system. If the cofactor for oxidative metabolism, NADPH, is not added, the gaseous trichloroethylene rapidly equilibrates with the microsomal suspension. Addition of NADPH results in a further uptake of 14C-trichloroethylene from the gas phase, linearly with time, which is due to enzymic metabolism. This part of uptake is inhibited by some arylimidazoles and 1.2.3-benzothiadiazoles. The compounds of greatest inhibitory potency were 6-chloro-1.2.3-benzothiadiazole and 5,6-dimethyl-1.2.3-benzothiadiazole. Part of.the metabolites of 14C-trichloroethylene formed by rat liver microsomes were irreversibly bound to microsomal protein, amounting up to 1 nmol per mg microsomal protein per hour. Model experiments on uptake of 14C-trichloroethylene from the gas phase by albumin solutions and liposomal suspensions (from lecithin) showed a rapid equilibration of trichloroethylene also with these systems. Comparison with previous analogous data on vinyl chloride revealed an about 10 times higher affinity of trichloroethylene to albumin and lipid, consistent with the behaviour of both compounds in the rat liver microsomal system.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00380890
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