NIOSHTIC-2 Publications Search
Delta-aminolevulinate dehydratase, a zinc dependent enzyme.
Finelli VN; Murthy L; Peirano WB; Petering HG
Biochem Biophys Res Commun 1974 Jan; 60(4):1418-1424
Erythrocyte and liver tissue delta-aminolevulinate dehydratase activity is determined in rats fed a semipurified diet under controlled nutritional intake of zinc (7440666) and copper (7440508). A significant decrease in enzymatic activity is observed in animals fed a low zinc diet, while dietary copper has no effect. In vitro addition of zinc to the erythrocyte preparations obtained from rats on low zinc diet produces a slight increase in enzymatic activity. Though zinc is the metal ion activator of the enzyme, the requirement of zinc is at the site of enzyme synthesis.
NIOSH-Publication; NIOSH-Grant; Enzyme-activity; Metallic-ions; Heavy-metals
Environmental Health Kettering Laboratory Eden & Bethesda Avenues Cincinnati, Ohio 45219
Issue of Publication
Biochemical and Biophysical Research Communications
University of Cincinnati, Cincinnati, Ohio
Page last reviewed: November 20, 2020
Content source: National Institute for Occupational Safety and Health Education and Information Division