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Abstract
The interaction of 210Pb of high specific activity with constituents of blood was investigated. In vivo experiments using 210Pb were performed in beagles and in vitro studies were done with human and canine whole blood and isolated blood cells. About 90 % of the nuclide found with red cells was associated with cytoplasm and less than 10 % was bound to the stroma. Transfer of 210Pb across the red cell membrane did not require the presence of plasma proteins. Gel electrophoresis of red cell cytoplasm showed that most of the 210Pb was present in the fractions that also contained hemoglobin. In the dog varying amounts were also found in fractions that had electrophoretic mobilities greater than hemoglobin. The HbA2 (alpha2delta2) component of fresh human hemoglobin had a much higher affinity for 210Pb than the main HbA (alpha2beta2) fraction. When stable lead was added to the 210Pb, the HbA2 component was saturated, and a larger fraction of the lead was found with the main hemoglobin, HbA. Small amounts of 210Pb were also found with erythrocuprein.
Published Version
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