Restoration of lead-inhibited 5-aminolevulinate dehydratase activity in whole blood by heat, zinc ion, and (or) dithiothreitol.
We examined effects of heat, zinc, ion, and dithiothreitol in restoring the activity of lead-inhibited-5-aminolevulinate dehydratase (EC 4.2.1.24). The ratio of non-activated to activated activity produced by dithiothreitol correlated well with blood lead concentration among 35 lead workers. The individual effects of heat, zinc, or dithiothreitol differ from each other in the shift of pH optimum as well as in the extent to which activity is restored. Dual or triple combinations of these agents show additive or complementary restoration of activity. The combination of heat and zinc or zinc and dithiothreitol expands the range of optimum concentration of zinc in restoring activity. Using these combinations of agents, we can expect more accurate evaluation of lead exposure than by measuring only activation of zinc. Although dithiothreitol most powerfully restores activity, it restores not only the activity inhibited by lead exposure but also the activity removed by oxidation of SH-groups in the enzyme molecule.
D004229:Dithiothreitol; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007854:Lead / Q000097:blood*; D007855:Lead Poisoning / Q000097:blood / Q000201:enzymology; D000623:Porphobilinogen Synthase / Q000037:antagonists & inhibitors / Q000097:blood*; D015032:Zinc
D007854:Lead; D000623:Porphobilinogen Synthase; D015032:Zinc; D004229:Dithiothreitol