Serum protein binding of lead in vitro in amyotrophic lateral sclerosis patients and controls.

The binding of lead to serum proteins was studied in vitro in ALS-patients and controls. Serum was incubated with 210Pb, the proteins were separated by isoelectric focusing and the radioactivity in the different protein fractions was determined by liquid scintillation counting. The activity was concentrated in the orosomucoid (acid alpha1-glycoprotein) fraction both in ALS-patients and controls under the present experimental conditions and the capacity of this protein to bind lead was demonstrated in a control experiment. The findings are discussed in relation to our earlier observations on increased concentrations of lead in cerebrospinal fluid and plasma in ALS-patients and the hypothetical role of the retrograde axonal transport in motoneurons in the pathogenesis of ALS. The present observations do not lend support to the idea that the increased plasma concentrations of lead in the disease would be related to qualitative differences in serum protein binding.