The uptake of metallic mercury by peroxidase in animals and its inhibition by L-dopa.

The uptake of metallic mercury by lactoperoxidase was measured. The results are described as follows: (1) The uptake of metallic mercury by lactoperoxidase in the presence of hydrogen peroxide was 10 times higher than that in the absence of hydrogen peroxide. (2) The uptake of metallic mercury by lactoperoxidase in the presence of L-dopa in the Lact. -H(2)O(2) system decreased, and decreased further as the concentration of L-dopa increased. (3) The uptake of metallic mercury by lactoperoxidase in the Lact. -H(2)O(2) system showed a tendency to increase, when the concentration of hydrogen peroxide increased. (4) The uptake of metallic mercury by lactoperoxidase increased with an increase in the lactoperoxidase concentration when the concentration of L-dopa and H(2)O(2) in the Lact. -L-dopa-H(2)O(2) system was constant. This uptake was similar in value to the increase changed by increase in the concentration of hydrogen peroxide