The effect of lead on the activities of erythrocyte pyrimidine 5′-nucleotidase (Py5N) and delta-aminolevulinate dehydratase (ALA-D) was studied in the mice which were given ad libitum a drinking water containing lead of 10, 50 and 250 ppm, for 27 days. The erythrocyte Py5N activity was not decreased in all groups of lead-exposed mice. However, the erythrocyte ALA-D activity was markedly decreased in the groups exposed to 50 and 250 ppm lead. These data indicate that erythrocyte ALA-D is more sensitive than Py5N to lead in vivo.
On the other hand, from the in vitro study, it was demonstrated that the human erythrocyte Py5N is moderately inhibited by zinc and tin, and markedly by mercury, cadmium, silver, copper, and lead, at 10−4 molar concentrations. In addition, it was observed that the erythrocyte Py5N is most remarkably inhibited by mercury while the ALA-D by lead, among metals tested.
Lead-exposed mice Erythrocyte Py5N activity Erythrocyte ALA-D activity In vitro inhibition by metals
This is a preview of subscription content, log in to check access
Hernberg S, Tola S, Nikkanen J, Valkonen S (1972) Erythrocyte deltaaminolevulinic acid dehydratase in new lead exposure. Arch Environ Health 25:109–113PubMedGoogle Scholar
Nikkanen J, Hernberg S, Tola S (1972) Modifications of the delta-aminolevulinic acid dehydratase test and their significance for assessing different intensities of lead exposure. Work Environ Health 9:46–52Google Scholar
Paglia DE, Valentine WN (1975) Characteristics of a pyrimidine-specific 5′-nucleotidase in human erythrocytes. J Biol Chem 250:7973–7979PubMedGoogle Scholar
Paglia DE, Valentine WN, Fink K (1977) Lead poisoning: Further observations on erythrocyte pyrimidine-nucleotidase deficiency and intracellular accumulation of pyrimidine nucleotides. J Clin Invest 60:1362–1366PubMedCrossRefGoogle Scholar
Rosa R, Valentine C, Rosa J (1977) Electrophoretic characterization of pyrimidine 5′-nucleotidase of human erythrocytes and its distinction from acid phosphatase. Clin Chim Acta 79:115–118CrossRefPubMedGoogle Scholar
Sano S (1955) Studies on the nature of basophilic stippled cell in lead poisoning. Report 1. Studies on the cytological investigation of basophilic stippled cell, Acta Haematol Jpn 18:625–630CrossRefGoogle Scholar
Satoh Y, Sasaki T, Yasuda H, Taniguchi N, Saito K (1979) Effect of lead on erythrocyte pyrimidine 5′-nucleotidase activity (in Japanese). Jap J Hyg 34:139Google Scholar
Takahashi T (1957) The determination of phosphoric compounds (in Japanese), Protein Nucl Acid Enzyme 2:464–468Google Scholar
Tola S, Hernberg S, Asp S, Nikkanen J (1973) Parameters indicative of absorption and biological effect in new lead exposure: a prospective study. Br. J. Ind. Med. 30:134–141PubMedGoogle Scholar
Tomokuni K, Ogata M (1976) Relationship between lead concentration in blood and biological response for porphyrin metabolism in workers occupationally exposed to lead. Arch Toxicol 35:239–246CrossRefPubMedGoogle Scholar
Valentine WN, Fink K, Paglia DE, Harris SR, Adams WS (1974) Hereditary hemolytic anemia with human erythrocyte pyrimidine 5′-nucleotidase deficiency. J Clin Invest 54:866–879PubMedGoogle Scholar