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. 1981 May;32(2):427–431. doi: 10.1128/iai.32.2.427-431.1981

Some enzymatic characteristics of eosinophil peroxidase from patients with eosinophilia and from healthy donors.

A J Bos, R Wever, M N Hamers, D Roos
PMCID: PMC351460  PMID: 6265355

Abstract

Some enzymatic characteristics of human eosinophil peroxidase were compared with those of human myeloperoxidase. Both enzymes catalyzed the oxidation of iodide by hydrogen peroxide. This assay proved to be very sensitive; the activity of 100 eosinophils/ml could be measured. The position of the pH optimum of this reaction was linearly dependent on the logarithm of the iodide/H2O2 ratio. At the same substrate ratio, this optimum was about 1 pH unit higher for eosinophil peroxidase than for myeloperoxidase. This difference may be related to the action of myeloperoxidase inside an acidified phagolysosome as opposed to the extracellular action of eosinophil peroxidase on the surface of certain parasites. Under defined conditions (KI, 1.4 mM; H2O2, 0.18 mM; cetyltrimethylammonium bromide, 0.008% [wt/vol]; pH 6), the activity of eosinophil peroxidase could be measured in a mixed granulocyte suspension independently of myeloperoxidase. Eosinophils from patients with eosinophilia were found to contain as much peroxidase activity as did eosinophils from healthy donors. No enzymatic differences in eosinophil peroxidase were found between the two types of donors.

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Selected References

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  1. Bakkenist A. R., Wever R., Vulsma T., Plat H., van Gelder B. F. Isolation procedure and some properties of myeloperoxidase from human leucocytes. Biochim Biophys Acta. 1978 May 11;524(1):45–54. doi: 10.1016/0005-2744(78)90101-8. [DOI] [PubMed] [Google Scholar]
  2. Bakkenist A. R., de Boer J. E., Plat H., Wever R. The halide complexes of myeloperoxidase and the mechanism of the halogenation reactions. Biochim Biophys Acta. 1980 Jun 13;613(2):337–348. doi: 10.1016/0005-2744(80)90088-1. [DOI] [PubMed] [Google Scholar]
  3. Bass D. A., Grover W. H., Lewis J. C., Szejda P., DeChatelet L. R., McCall C. E. Comparison of human eosinophils from normals and patients with eosinophilia. J Clin Invest. 1980 Dec;66(6):1265–1273. doi: 10.1172/JCI109978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bos A., Wever R., Roos D. Characterization and quantification of the peroxidase in human monocytes. Biochim Biophys Acta. 1978 Jul 7;525(1):37–44. doi: 10.1016/0005-2744(78)90197-3. [DOI] [PubMed] [Google Scholar]
  5. Butterworth A. E., David J. R., Franks D., Mahmoud A. A., David P. H., Sturrock R. F., Houba V. Antibody-dependent eosinophil-mediated damage to 51Cr-labeled schistosomula of Schistosoma mansoni: damage by purieid eosinophils. J Exp Med. 1977 Jan 1;145(1):136–150. doi: 10.1084/jem.145.1.136. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Caulfield J. P., Korman G., Butterworth A. E., Hogan M., David J. R. The adherence of human neutrophils and eosinophils to schistosomula: evidence for membrane fusion between cells and parasites. J Cell Biol. 1980 Jul;86(1):46–63. doi: 10.1083/jcb.86.1.46. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Desser R. K., Himmelhoch S. R., Evans W. H., Januska M., Mage M., Shelton E. Guinea pig heterophil and eosinophil peroxidase. Arch Biochem Biophys. 1972 Feb;148(2):452–465. doi: 10.1016/0003-9861(72)90164-6. [DOI] [PubMed] [Google Scholar]
  8. Fabian I., Aronson M. Deamination of histamine by peroxidase of neutrophils and eosinophils. J Reticuloendothel Soc. 1975 Mar;17(3):141–145. [PubMed] [Google Scholar]
  9. Glauert A. M., Butterworth A. E., Sturrock R. F., Houba V. The mechansim of antibody-dependent, eosinophil-mediated damage to schistosomula of Schistosoma mansoni in vitro: a study by phase-contrast and electron microscopy. J Cell Sci. 1978 Dec;34:173–192. doi: 10.1242/jcs.34.1.173. [DOI] [PubMed] [Google Scholar]
  10. Grove D. I., Mahmoud A. A., Warren K. S. Eosinophils and resistance to Trichinella spiralis. J Exp Med. 1977 Mar 1;145(3):755–759. doi: 10.1084/jem.145.3.755. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Jong E. C., Mahmoud A. A., Klebanoff S. J. Peroxidase-mediated toxicity to schistosomula of Schistosoma mansoni. J Immunol. 1981 Feb;126(2):468–471. [PubMed] [Google Scholar]
  12. Klebanoff S. J., Hamon C. B. Role of myeloperoxidase-mediated antimicrobial systems in intact leukocytes. J Reticuloendothel Soc. 1972 Aug;12(2):170–196. [PubMed] [Google Scholar]
  13. Lehrer R. I., Cline M. J. Leukocyte myeloperoxidase deficiency and disseminated candidiasis: the role of myeloperoxidase in resistance to Candida infection. J Clin Invest. 1969 Aug;48(8):1478–1488. doi: 10.1172/JCI106114. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Mahmoud A. A., Warren K. S., Peters P. A. A role for the eosinophil in acquired resistance to Schistosoma mansoni infection as determined by antieosinophil serum. J Exp Med. 1975 Oct 1;142(4):805–813. doi: 10.1084/jem.142.4.805. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. McLaren D. J., Mackenzie C. D., Ramalho-Pinto F. J. Ultrastructural observations on the in vitro interaction between rat eosinophils and some parasitic helminths (Schistosoma mansoni, Trichinella spiralis and Nippostrongylus brasiliensis). Clin Exp Immunol. 1977 Oct;30(1):105–118. [PMC free article] [PubMed] [Google Scholar]
  16. Migler R., DeChatelet L. R. Human eosinophilic peroxidase: biochemical characterization. Biochem Med. 1978 Feb;19(1):16–26. doi: 10.1016/0006-2944(78)90003-0. [DOI] [PubMed] [Google Scholar]
  17. Paul B., Sbarra A. J. The role of the phagocyte in host-parasite interactions. 13. The direct quantitative estimation of H2O2 in phagocytizing cells. Biochim Biophys Acta. 1968 Feb 1;156(1):168–178. doi: 10.1016/0304-4165(68)90116-5. [DOI] [PubMed] [Google Scholar]
  18. Salmon S. E., Cline M. J., Schultz J., Lehrer R. I. Myeloperoxidase deficiency. Immunologic study of a genetic leukocyte defect. N Engl J Med. 1970 Jan 29;282(5):250–253. doi: 10.1056/NEJM197001292820505. [DOI] [PubMed] [Google Scholar]
  19. Weening R. S., Roos D., Loos J. A. Oxygen consumption of phagocytizing cells in human leukocyte and granulocyte preparations: a comparative study. J Lab Clin Med. 1974 Apr;83(4):570–577. [PubMed] [Google Scholar]
  20. West B. C., Gelb N. A., Rosenthal A. S. Isolation and partial characterization of human eosinophil granules. Comparison to neutrophils. Am J Pathol. 1975 Dec;81(3):575–588. [PMC free article] [PubMed] [Google Scholar]
  21. Wever R., Hamers M. N., Weening R. S., Roos D. Characterization of the peroxidase in human eosinophils. Eur J Biochem. 1980 Jul;108(2):491–495. doi: 10.1111/j.1432-1033.1980.tb04746.x. [DOI] [PubMed] [Google Scholar]
  22. Wever R., Plat H., Hamers M. N. Human eosinophil peroxidase: a novel isolation procedure, spectral properties and chlorinating activity. FEBS Lett. 1981 Jan 26;123(2):327–331. doi: 10.1016/0014-5793(81)80320-1. [DOI] [PubMed] [Google Scholar]
  23. Zgliczynski J. M., Selvaraj R. J., Paul B. B., Stelmaszynska T., Poskitt P. K., Sbarra A. J. Chlorination by the myeloperoxidase-H2O2-Cl- antimicrobial system at acid and neutral pH. Proc Soc Exp Biol Med. 1977 Mar;154(3):418–422. doi: 10.3181/00379727-154-39684. [DOI] [PubMed] [Google Scholar]

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