In-vitro experiments using 203Pb were performed to identify the lead binding components in human peripheral blood. The distribution of lead in plasma, in the red cell membrane, and within the red cell was also investigated. Studies of the distribution of 203Pb in whole blood showed that at a lead concentration of 2 45 ,umol/l (50 ug/100 ml) about 94 % of lead had been incorporated by the erythrocytes and 6 % remained in the plasma. responsible for the lead uptake; one is protein and the other a non-protein, probably a phenolic compound. This hypothesis has been discounted by Clarkson and Kench,4 who suggested that lead exists in the blood as a peptised lead phosphate-sol, the groups of which are probably aggregated on the surface of the cell to form a larger particulate. On the other hand, recent studies by Barltrop and Smith7 8 using tracer 203Pb do not confirm that lead has an affinity to the red blood cell membrane. These authors separated the 203Pb-containing fraction of RBC by sephadex gel filtration and ultracentrifugation. Lead was found attached to the intracellular constituents rather than the stromal membrane, and to a molecule similar in size to the haemoglobin polypeptide. White,9 however, and Selhi and White'0 believe that the attachment takes place in the erythrocyte membrane, which results in alteration of membrane protein conformation.The identification of specific lead binding sites in the blood is hindered by experimental difficulties such as the necessity to detect and to measure trace amounts of lead in microsamples of subcellular 78