Skip to main content
Log in

Delta aminolevulinic acid dehydratase amounts in lead-exposed subjects: description of a method correlated with the immunoturbidimetric assay

  • Original Papers
  • Published:
International Archives of Occupational and Environmental Health Aims and scope Submit manuscript

Summary

The measurement of δ-aminolevulinic acid dehydratase (ALA.D) activity is a good index of lead exposure. Recently, we proposed an immunotubidimetric assay which allows determination of the amount of the enzyme. This last test is particularly interesting for workers presenting high blood-lead levels. We then studied the effects of different agents (dithiothreitol, heat and zinc ions) in restoring the activity of lead-inhibited ALA.D. The individual or combined effects of these three agents showed an additive restoration of activity. The combination of zinc ions with heat and/or DTT gave the best activations, which correlated perfectly with ALA.D amounts. Consequently, the catalytic assay using zinc ions and DTT may be used in routine testing as an indirect measurement of ALA.D amount.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Barnard GF, Itoh R, Hohberger LH, Shemin D (1977) Mechanism of porphobilinogen synthase. Possible role of essential thiol groups. J Biol Chem 252:8965–8974

    Google Scholar 

  2. Berlin A, Schaller KM (1977) European standardized method for the determination of S aminolevulinic acid dehydratase activity in blood. J Clin Chem Clin Biochem 12:389–390

    Google Scholar 

  3. Border EA, Caltrell AC, Kilroe TA (1972) The in vitro effect of zinc on the inhibition of human δ aminolevulinic acid dehydratase by lead. Br J Ind Med 33:36–42

    Google Scholar 

  4. Boudene C, Despaux-Pagès N, Comoy E, Bohuon C (1984) Immunological and enzymatic studies of erythrocytic δ aminolevulinate dehydratase: comparison of results obtained in normal and lead exposed subjects. Int Arch Occup Environ Health 55:87–96

    Google Scholar 

  5. Candura F, Franco G, Pozzi U (1971) Influenza del calore sull'attivita ALA deidratasica eritrocitaria nell conigho et nell uomo. Lav Um 23:1–10

    Google Scholar 

  6. Chiba M (1972) Activity of erythrocyte δ aminolevulinic acid dehydratase and its change by heat treatment as indices of lead exposure. Br J Ind Med 33:36–42

    Google Scholar 

  7. Despaux N, Bohuon C, Comoy E, Boudene C (1977) Postulated mode of action of metals on purified human ALA dehydratase. Biomedicine 27:358–361

    Google Scholar 

  8. Despaux N, Comoy E, Bohuon C, Boudene C (1979) Purification and properties of human erythrocyte delta aminolevulinic acid dehydratase. Biochimie 61:1021–1028

    Google Scholar 

  9. Despaux-Pagès N, Comoy E, Bohuon C, Boudene C (1985) Immunoturbidimetric assay of δ aminolevulinic acid dehydratase (ALA.D) on a centrifugal fast analyser. Clin Chim Acta 147:179–181

    Google Scholar 

  10. Despaux-Pagès N, Comoy E, Bohuon C, Boudene C (1986) Activated porphobilinogen synthase (PBS) activities as an indirect determination of PBS amounts in healthy subjects — Accepted for publication in Clin Chem

  11. Doss M, Becker U, Geisse S, Solcher H, Schneider J, Kufner G, Schlegel H, Stoeppler N (1982) Persistent protophorynemia in hereditary porphobiligen synthase (ALA.D) deficiency under low lead exposure. A new molecular basis for the pathogenesis of lead intoxication. Klin Wochenschr 60:599–606

    Google Scholar 

  12. Granick JL, Sassa S, Granick S, Levere RD, Kappas A (1973) Studies in lead poisoning. II. Correlation between the ratio of activated to inactivated δ aminolevulinic acid dehydratase of whole blood and the blood lead level. Biochem Med 8:149–159

    Google Scholar 

  13. Haas T, Mache W, Schaller K, Mache K, Klavis G, Stumpf R (1972) Zur Bestimmung der Delta-Aminolävulinsäure-Dehydratase und ihrer diagnostischen Wertigkeit. Int Arch Arbeitsmed 30:87–104

    Google Scholar 

  14. Hapke HJ, Prigge E (1973) Interactions of lead and glutathione with delta aminolevulinic acid dehydratase. Arch Toxicol 31:153–161

    Google Scholar 

  15. Meredith PA, Moore MR, Goldberg A (1977) Effects of aluminium, lead and zinc on S aminolevulinic acid dehydratase. Enzyme 22:22–27

    Google Scholar 

  16. Mitchell RA, Drake JE, Wittlin LA, Rejint TA (1977) Erythrocyte porphobilinogen synthase (delta-aminolevulin ate dehydratase) activity: a reliable and quantitative indicator of lead exposure in humans. Clin Chem 23:105–111

    Google Scholar 

  17. Sakai T, Yanagihara S, Ushio K (1980) Restoration of lead inhibited 5-aminolevulinate dehydratase activity in whole blood by heat, zinc ion, and (or) dithiothreitol. Clin Chem 26:625–628

    Google Scholar 

  18. Tomokuni K, Kawanishi T (1975) Relationships between activation of delta aminolevulinic acid dehydratase by heating and blood lead level. Arch Toxicol 34:253–258

    Google Scholar 

  19. Trevisan A, Gori GP, Zangirolami A, Benvenutto C, Rosa A Chiesura P (1980) Site of action of metals on the aminolevulinic acid dehydratase of human erythrocytes. Enzyme 25:33–36

    Google Scholar 

  20. Tsukamoto I, Yoshinaga T, Sano S (1980) Zinc and cysteine residues in the active site of bovine liver δ aminolevulinic acid dehydratase. Int J Biochem 12:751–756

    Google Scholar 

  21. Werner C, Krebs B, Keith G, Dirheimer G (1976) Specific cleavages of pure tRNAs by plumbous ions. Biochem Biophys Acta 432:161–175

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Despaux-Pagès, N., Comoy, E., Bohuon, C. et al. Delta aminolevulinic acid dehydratase amounts in lead-exposed subjects: description of a method correlated with the immunoturbidimetric assay. Int. Arch Occup Environ Heath 57, 303–313 (1986). https://doi.org/10.1007/BF00406185

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00406185

Key words

Navigation