Erythrocyte porphobilinogen synthase (delta-aminolaevulinate dehydratase) activity: a reliable and quantitative indicator of lead exposure in humans.

Abstract

Abstract We assessed optimal conditions for assay of porphobillinogen synthase (EC 4.2.1.24) activity in human blood containing abnormally high concentrations of lead. Zn2+and -SH, both required for complete activation of the enzyme, had additive effects. Using a modified method based on these studies, we found blood lead concentration to be strictly proportional to ln(activated/nonactivated) enzyme activity. One brand of commercially available "lead-free" tubes contained a substance that interfered with this relationship. In vitro studies, with the modified assay, showed ALAD to be activated by low concentrations but inactivated by high concentrations of Hg2+, Cd2+, and ethylenediaminetetraacetate. We fouund no genetically influenced differences among unexposed individuals when in(activated/nonactivated) enzyme activities were compared. The technique is suitable for use in screening for lead poisoning in humans.