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Relationships between distribution of lead in erythrocytes in vivo and in vitro and inhibition of ALA-D.
  1. T Sakai,
  2. S Yanagihara,
  3. Y Kunugi,
  4. K Ushio

    Abstract

    Proteins in the ALA-D (delta-aminolaevulinic acid dehydratase) fraction from gel filtration of erythrocyte supernatant (ES) have the highest affinity for lead among erythrocyte constituents in vivo and in vitro. It takes 20-40 hours for erythrocyte components to be equilibrated with lead added in vitro. AT low lead concentrations, under 60 micrograms/100 ml ES, the extent of decrease in ALA-D activity indicates the extent of lead saturation of ALA-D fraction proteins. The saturation is attained at 80-110 micrograms/100 ml ES. Although an appreciable amount of lead is also found in the haemoglobin fraction that contains certain factors concerned in ALA-D inhibition, lead responsible for inducing the inhibition is not bound to haemoglobin fraction proteins but to ALA-D fraction proteins. Of three treatments or agents recovering the enzyme from lead effects, zinc is the only one that can fully restore the inhibition.

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