Abstract
Administration of a sublethal dose of lead acetate to rats induced the simultaneous synthesis of a Pb-metallothionein (Pb-MT)-like protein (Pb-BP) and Zn-thionein (Zn-BP) in the liver. The Pb-BP had an apparent molecule mass of 6900 Da and seemed to bind preferentially to lead in the liver cytosol. The Zn-BP was identified by comparison of the Mr, elution profiles from Sephadex G-75 and DEAE-Sephadex A-25 columns, and polyacrylamide-gel-electrophoretic mobility, with those of rat liver Zn-MT-II. The Pb-BP accumulated in the liver to a maximum 6 h after the intraperitoneal injection of lead acetate and accounted for about 60% of the lead in the liver cytosol at this stage. However, after that, it gradually decreased in the liver, until it was close to the basal amount 24 h after the induction. In contrast, the amount of Zn-MT increased gradually, reached a maximum 12 h after the administration of lead acetate and maintained a constant value until at least 24 h after the induction. Amino acid analysis of the Pb-BP indicated that it contained about 28% half-cysteine. These results strongly suggest that lead acetate induces the synthesis of Pb-MT as well as Zn-MT in rat liver.