Formation of dityrosine by human salivary lactoperoxidase in vitro

References

• Aeschbach R. Die Bildung von Dityrosin in proteinen durch Oxidation von Tyrosinresten. Acad. Diss., Zurich 1975
   Google Scholar
• Andersen S. Characterization of a new type of cross linkage in resilin, a rubber-like protein. Biochem, Biophys. Acta 1963; 69: 249–262
   PubMed Web of Science ®Google Scholar
• Bayse G. S., Michaels A. W., Morrison M. The peroxidase-catalyzed oxidation of tyrosine. Biochem. Biophys. Acta 1972; 284: 34–42
   PubMed Web of Science ®Google Scholar
• Chance B., Maehly A. C. Methods in Enzymology. Academic Press, New York 1964; Vol. II: 764
   Google Scholar
• Hoogendoorn H. The effect of lactoperoxidase-thiocyanate-hydrogen peroxide on the metabolism of cariogenic micro-organisms in vitro and in the oral cavity. Acad. Diss., Haag 1974
   Google Scholar
• Hoogendoorn H., Piessens J. P., Scholtes W., Stoddard L. A. Hypothiocyanite ion; The inhibitor formed by the system lactoperoxidase-thiocyanate-hydrogen peroxide. Caries Res. 1977; 11: 77–84
   PubMed Web of Science ®Google Scholar
• Hosoya T. Effect of various reagents including antithyroid compounds upon the activity of thyroid peroxidase. J. Biochem. (Tokyo) 1963; 53: 381–388
   PubMedGoogle Scholar
• Klebanoff S. J., Luebke R. G. The anti-lactobacillus system of saliva. Role of salivary peroxidase. Proc. Soc. exp. Biol. Med. 1965; 118: 483–486
   PubMed Web of Science ®Google Scholar
• Kraus F. W., Nickerson J. F., Perry W. I., Walker A. P. Peroxide and peroxidogenic bacteria in human saliva. J. Bacteriol. 1957; 73: 727–735
   PubMedGoogle Scholar
• LaBella F., Keeley F., Vivian S., Thornhill D. Evidence for dityrosine in elastin. Biochem. Biophys. Res. Commun. 1967; 26: 748–753
   PubMed Web of Science ®Google Scholar
• LaBella F., Waykole P., Queen G. Formation of insoluble gels and dityrosine by the action of peroxidase on soluble collagens. Biochem. Biophys. Res. Commun. 1968; 30: 333–338
   PubMed Web of Science ®Google Scholar
• Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. Protein measurement with the folin phenol reagent. J. Biol. Chem. 1951; 193: 265–275
   PubMed Web of Science ®Google Scholar
• Marchalonis J. J. An enzymic method for the trace iodination of immunoglobulins and other proteins. Biochem. J. 1969; 113: 299–305
   PubMed Web of Science ®Google Scholar
• Morrison M., Steele W. F. Lactoperoxidase, the peroxidase in the salivary gland. Biology of the Mouth, P. Person, Washington 1968; 89–110
   Google Scholar
• Mäkinen K. K., Tenovuo J. Chromatographic separation of human salivary peroxidases. Acta Odontol. Scand. 1976; 34: 141–150
   PubMed Web of Science ®Google Scholar
• Mäkinen K. K., Tenovuo J., Scheinin A. Xylitol-induced increase of lactoperoxidase activity. J. Dent. Res. 1976; 55: 652–660
   PubMed Web of Science ®Google Scholar
• Mäkinen K. K., Bowen W. H., Dalgard D., Fitzgerald G. Effect of peroral administration of xylitol on exocrine secretions of monkeys. J. Nutr. 1978; 108: 779–789
   PubMedGoogle Scholar
• Mäkinen K. K., Tenovuo J. The effect of peroral administration of xylitol on human milk, Unpublished results
   Google Scholar
• Pande C. S., McMenamy R. H. Thiocyanate binding with modified bovine plasma albumins. Arch. Biochem. Biophys. 1970; 136: 260–267
   PubMedGoogle Scholar
• Sarimo S. S., Tenovuo J. Enzymatically iodinated human salivary proteins. Fractionation and characterization by column chromatography and electrofocusing. Biochem. J. 1977; 167: 23–29
   PubMedGoogle Scholar
• Stahmann M. A., Spencer A. K. Deamination of protein lysyl e-amino groups by peroxidase in vitro. Biopolymers 1977; 16: 1299–1306
   PubMedGoogle Scholar
• Stahmann M. A., Spencer A. K., Honold G. R. Cross linking of proteins in vitro by peroxidase. Biopolymers 1977; 16: 1307–1318
   PubMed Web of Science ®Google Scholar
• Tenovuo J. The peroxidatic activity in the human oral cavity. Acta Odontol. Scand. 1976; 34(Suppl. 71)
   Google Scholar
• Tenovuo J., Mäkinen K. K. Concentration of thiocyanate and ionizable iodine in saliva of smokers and non-smokers. J. Dent. Res. 1976; 55: 661–663
   PubMed Web of Science ®Google Scholar
• Tenovue J., Sarimo S. S. Enzymatic iodination of salivary proteins by the 125I-lactoperoxidase system. Scand. J. Dent. Res. 1977; 85: 355–361
   PubMedGoogle Scholar
• Tenovuo J. Lactoperoxidase-catalysed iodine metabolism in human saliva. Archs oral Biol. 1978; 23: 253–258
   PubMedGoogle Scholar
• Tenovuo J. Inhibition by thiocyanate of lactoperoxidase-catalysed oxidation and iodination reactions. Archs oral. Biol. 1978; 23: 899–903
   PubMedGoogle Scholar
• Tenovuo J., Paunio K. Peroxidase-catalysed formation of dityrosine, a protein crosslink, in human periodontal ligament collagen, Unpublished results
   Google Scholar
• Waykole P., Heidemann E. Dityrosine in collagen, Conn. Tiss. Res. 1976; 4: 219–222
   Google Scholar
• Wood J. L. Chemistry and Biochemistry of Thiocyanic Acid and its Derivatives, A. A. Newmann. Academic Press, London 1975; 156–221
   Google Scholar