A low-molecular-weight protein was measured in erythrocytes from workers with chronic and recent lead exposure, with and without clinical lead toxicity, and from a group of control subjects not exposed to undue environmental lead. The protein was detected in all the workers, but in significantly smaller amounts in those with symptoms, and was absent from controls. The synthesis of the protein is induced at blood lead concentrations above 1.9 mumol/L, but is reduced in workers susceptible to clinical lead toxicity at blood lead concentrations below 4.0 mumol/L. The activity of the red blood cell dithiothreitol (DTT)--activated 5-aminolaevulinate dehydratase (ALA-D) was correlated with the concentration of the low-molecular-weight protein, with both being particularly low in the symptomatic workers. Previous studies have shown that the protein binds lead. By sequestrating excess lead into a non-toxic form, the protein may have a protective role in preventing clinical, and reducing biochemical, lead toxicity.