Abstract
Rat erythrocyte δ-aminolevulinate dehydratase (ALA-D) has been confirmed to be an enzyme dependent on dietary zinc. Levels of blood ALA-D decreased substantially during the first five weeks after weaning and remained constant thereafter. Dietary lead (200 ppm) caused a dramatic fall in erythrocyte ALA-D activity and, following the removal of lead exposure, the return of the enzymatic activity toward normal values was quicker in the animals receiving higher zinc than in those on lower zinc diet. Furthermore, invitro addition of zinc to erythrocyte preparation obtained from rats exposed to dietary lead reactivated ALA-D to control values. Maximal enzymatic activity in both lead-fed and control animals occurred at 10−4M ZnCl2. There seems to be a competition between Pb++ and Zn++ in binding to the enzyme, with Pb++ as inhibitor and Zn++ as activator.
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