Skip to main content
NCBI home page
Journal of Clinical Microbiology logoLink to Journal of Clinical Microbiology
. 1983 Nov;18(5):1177–1182. doi: 10.1128/jcm.18.5.1177-1182.1983

Evidence for thiocyanate-sensitive peroxidase activity in human saliva.

R A Cowman, S S Baron, S D Obenauf, J J Byrnes
PMCID: PMC272863  PMID: 6315768

Abstract

A procedure was developed for determining the relative levels of lactoperoxidase, leukocyte myeloperoxidase, and thiocyanate-sensitive peroxidase in human saliva. With this procedure, most of the peroxidase activity in whole saliva from normal (those without cancer) subjects was found to be associated with lactoperoxidase and thiocyanate-sensitive peroxidase, with only a minor contribution from leukocyte myeloperoxidase. In contrast, thiocyanate-sensitive peroxidase and leukocyte myeloperoxidase were the major peroxidase activities present in the residual salivary secretion obtainable from two xerostomic patients examined, and these enzymes were present at concentrations much higher than those normally occurring in human saliva. The occurrence of thiocyanate-sensitive peroxidase in saliva has not been previously reported and may represent either an additional peroxidase activity of saliva or a form of lactoperoxidase which is particularly sensitive to inhibition by thiocyanate.

Full text

PDF
1177

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  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. Brown L. R., Dreizen S., Daly T. E., Drane J. B., Handler S., Riggan L. J., Johnston D. A. Interrelations of oral microorganisms, immunoglobulins, and dental caries following radiotherapy. J Dent Res. 1978 Sep-Oct;57(9-10):882–893. doi: 10.1177/00220345780570090901. [DOI] [PubMed] [Google Scholar]
  3. Brown L. R., Dreizen S., Handler S., Johnston D. A. Effect of radiation-induced xerostomia on human oral microflora. J Dent Res. 1975 Jul-Aug;54(4):740–750. doi: 10.1177/00220345750540040801. [DOI] [PubMed] [Google Scholar]
  4. Brown L. R., O'Neill P. A., Dreizen S., Handler S. F., Riggan L. J., Perkins D. H. Relationship between saliva and serum agglutination titers and post-irradiation caries activity in cancer patients. J Dent Res. 1981 Jan;60(1):10–18. doi: 10.1177/00220345810600010101. [DOI] [PubMed] [Google Scholar]
  5. HOSOYA T., MORRISON M. THE PEROXIDASE AND OTHER HEMOPROTEINS OF THYROID MICROSOMES. Biochem Biophys Res Commun. 1965 Jun 18;20:27–32. [PubMed] [Google Scholar]
  6. Kersten H. W., Moorer W. R., Wever R. Thiocyanate as a cofactor in myeloperoxidase activity against Streptococcus mutans. J Dent Res. 1981 Apr;60(4):831–837. doi: 10.1177/00220345810600041201. [DOI] [PubMed] [Google Scholar]
  7. Klebanoff S. J. Myeloperoxidase-halide-hydrogen peroxide antibacterial system. J Bacteriol. 1968 Jun;95(6):2131–2138. doi: 10.1128/jb.95.6.2131-2138.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Llory H., Dammron A., Gioanni M., Frank R. M. Some population changes in oral anaerobic microorganisms, Streptococcus mutans and yeasts following irradiation of the salivry glands. Caries Res. 1972;6(4):298–311. doi: 10.1159/000259809. [DOI] [PubMed] [Google Scholar]
  9. Maguire R. J., Dunford H. B. Kinetics of the oxidation of iodide ion by lactoperoxidase compounds. II. Biochemistry. 1972 Feb 29;11(5):937–941. doi: 10.1021/bi00755a038. [DOI] [PubMed] [Google Scholar]
  10. Matheson N. R., Wong P. S., Travis J. Isolation and properties of human neutrophil myeloperoxidase. Biochemistry. 1981 Jan 20;20(2):325–330. doi: 10.1021/bi00505a015. [DOI] [PubMed] [Google Scholar]
  11. McRipley R. J., Sbarra A. J. Role of the phagocyte in host-parasite interactions. XII. Hydrogen peroxide-myeloperoxidase bactericidal system in the phagocyte. J Bacteriol. 1967 Nov;94(5):1425–1430. doi: 10.1128/jb.94.5.1425-1430.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Mäkinen K. K., Tenovuo J. Chromatographic separation of human salivary peroxidases. Acta Odontol Scand. 1976;34(3):141–150. doi: 10.3109/00016357609002561. [DOI] [PubMed] [Google Scholar]
  13. Mäkinen K. K., Tenovuo J., Scheinin A. Xylitol-induced increase of lactoperoxidase activity. J Dent Res. 1976 Jul-Aug;55(4):652–660. doi: 10.1177/00220345760550041901. [DOI] [PubMed] [Google Scholar]
  14. Pilz H., O'Brien J. S., Heipertz R. Human saliva peroxidase: microanalytical isoelectric fractionation and properties in normal persons and in cases with neuronal ceroid-lipofuscinosis. Clin Biochem. 1976 Apr;9(2):85–88. doi: 10.1016/s0009-9120(76)80023-9. [DOI] [PubMed] [Google Scholar]
  15. Tenovuo J. Different molecular forms of human salivary lactoperoxidase. Arch Oral Biol. 1981;26(12):1051–1055. doi: 10.1016/0003-9969(81)90116-3. [DOI] [PubMed] [Google Scholar]
  16. Tenovuo J., Knuuttila M. L. Antibacterial effect of salivary peroxidases on a cariogenic strain of Streptococcus mutans. J Dent Res. 1977 Dec;56(12):1608–1613. doi: 10.1177/00220345770560123301. [DOI] [PubMed] [Google Scholar]
  17. Tenovuo J. Lactoperoxidase-catalysed iodine metabolism in human saliva. Arch Oral Biol. 1978;23(4):253–258. doi: 10.1016/0003-9969(78)90014-6. [DOI] [PubMed] [Google Scholar]
  18. Tenovuo J., Valtakoski J. The correlation between salivary peroxidase activity, salivary flow rate, and the oxidation-reduction potentials of human saliva and dental plaque suspensions. Acta Odontol Scand. 1976;34(3):169–176. doi: 10.3109/00016357609002565. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Clinical Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES