Oxidative metabolism of propylthiouracil by peroxidases from rat bone marrow

References

• Agner K. Biological effects of hypochlorous acid formed by MPO‐peroxidation in the presence of chloride ions. In Structure and Function of Oxidation‐Reduction Enzymes, A. Akeson, A. Ehrewnberg. Pergamon Press. 1972; 329–335
   Google Scholar
• Allen R. C., Stjernholm R. J., Steele R. H. Evidence for the generation of an electronic excitation state(s) in human polymorphonuclear leukocytes and its participation in bactericidal activity. Biochemical and Biophysical Research Communication 1972; 47: 679–684
   PubMed Web of Science ®Google Scholar
• Allen R. C. Halide dependence of the myeloperoxidase‐mediated antimicrobial system of the polymorphonuclear leukocyte in the phenomenon of electronic excitation. Biochemical and Biophysical Research Communications 1975; 63: 675–683
   PubMed Web of Science ®Google Scholar
• Bartlett P. D., Altschul P. The polymerization of allyl compounds. II. Preliminary kinetics study of the peroxidase‐induced polymerization of allyl acetate. Journal of the American Chemical Society 1945; 67: 816–822
   Web of Science ®Google Scholar
• Davidson B., Soodak M., Neary J. T., Strout H. V., Kieffer J. D., Mover H., Maloof F. The irreversible inactivation of thyroid peroxidase by methylmercaptoimidazole, thiouracil, and propylthiouracil in vitro and its relationship to in vivo findings. Endocrinology 1978; 103: 871–882
   PubMed Web of Science ®Google Scholar
• Engler H., Taulog A., Nakashima T. Mechanism of inactivation of thyroid peroxidase by thioureylene drugs. Biochemical Pharmacology 1982; 31: 3801–3806
   PubMed Web of Science ®Google Scholar
• Hager L. P., Morris D. R., Brown F. S., Eberwein H. Chloroperoxidase II utilization of halogen anions. Journal of Biological Chemistry 1966; 241: 1769–1777
   PubMed Web of Science ®Google Scholar
• Kampmann J., Skovsted L. The pharmacokinetics of propylthiouracil. Acta Pharmacologica Toxicologica 1974; 35: 361–369
   PubMedGoogle Scholar
• Kariya K., Lee E., Hirouchi M. Relationship between leukopenia and bone marrow myeloperoxidase in the rat treated with propylthiouracil. Japanese Journal of Pharmacology 1984; 36: 217–222
   PubMedGoogle Scholar
• Kariya K., Sawahata T., Okuno S., Lee E. Inhibition of hepatic glutathione transferases by propylthiouracil and its metabolites. Biochemical Pharmacology 1986; 35: 1475–1479
   PubMed Web of Science ®Google Scholar
• Kariya K., Lee E., Hirouchi M., Hosokawa M., Sayo H. Purification and some properties of peroxidases of rat bone marrow. Biochimical et Biophysica Acta 1987; 911: 95–101
   PubMed Web of Science ®Google Scholar
• Klebanoff S. J. Myeloperoxidase‐halide‐H2O2 antibacterial system. Journal of Bacteriology 1968; 95: 2131–2138
   PubMed Web of Science ®Google Scholar
• Lam D. C. C., Lindsay R. H. Accumulation of 2‐‘14C’propylthiouracil in human polymorphonuclear leukocytes. Biochemical Pharmacology 1979a; 28: 2289–2296
   PubMed Web of Science ®Google Scholar
• Lam D. C. C., Lindsay R. H. Oxidation and binding of ‘2‐14C’propylthiouracil in human polymorphonuclear leukocytes. Drug Metabolism and Disposition 1979b; 7: 285–289
   PubMedGoogle Scholar
• Lindsay R. H., Kelly K., Hill J. B. Oxidative metabolites of ‘2‐14C’propylthiouracil in rat thyroid. Endocrinology 1979; 104: 1689–1697
   Google Scholar
• Marchant B., Alexander W. D., Robertson J. W. K., Lazarus J. H. Concentration of 35S‐propylthiouracil by the thyroid gland and its relationship to the anion trapping mechanism. Metabolism 1971; 20: 989–993
   PubMed Web of Science ®Google Scholar
• Matheson N. R., Wong P. S., Travis J. Enzymatic inactivation of human alpha‐1‐proteinase inhibitor by neutrophil myeloperoxidase. Biochemical and Biophysical Research Communications 1979; 88: 402–409
   PubMed Web of Science ®Google Scholar
• Neal R. A., Halpert J. Toxicology of thiono‐sulphur compounds. Annual Review of Pharmacology and Toxicology 1982; 22: 321–339
   PubMed Web of Science ®Google Scholar
• Odajima T. Oxidative destruction of the microbial metabolite aflatoxin by the myeloperoxidase‐hydrogen peroxide‐chloride system. Archives of Oral Biology 1981; 26: 339–340
   PubMedGoogle Scholar
• Paredes J. ‐M., Weiss S. J. Human neutrophils transform prostaglandins by a myeloperoxidase‐dependent mechanism. Journal of Biological Chemistry 1982; 257: 2738–2740
   PubMed Web of Science ®Google Scholar
• Rosen H., Klebanoff S. J. Formation of singlet oxygen by the myeloperoxidase‐mediated antimicrobial system. Journal of Biological Chemistry 1977; 252: 4803–4810
   PubMed Web of Science ®Google Scholar
• Sayo H., Hosokawa M., Lee E., Kariya K., Kohno M. ESR studies on the oxidation of N,N‐dimethyl‐p‐anisidine and its analogues catalyzed by myeloperoxidase. Biochimical et Biophysica Acta 1986; 874: 187–192
   PubMedGoogle Scholar
• Sitar D. S., Thornhill D. P. Propylthiouracil: Absorption, metabolism and excretion in the albino rat. Journal of Pharmacology and Experimental Therapeutics 1972; 183: 440–448
   PubMed Web of Science ®Google Scholar
• Taurog A. The mechanism of action of the thioureylene antithyroid drugs. Endocrinology 1976; 98: 1031–1046
   PubMed Web of Science ®Google Scholar
• Yamada M., Tsuda M., Nagao M., Mori M., Sugiura T. Degradation of mutagens from pyrolysates of tryptophan, glutamic acid and globlin by myeloperoxidase. Biochemical and Biophysical Research Communications 1979; 90: 769–776
   PubMedGoogle Scholar
• Yamada M., Mori M., Sugimura T. Myeloperoxidase‐catalyzed binding of 3‐amino‐1‐methyl‐5H‐pyrido‘4,3‐b’indole, a tryptophan pyrolysis product, to protein. Chemical‐Biological Interactions 1980; 33: 19–33
   PubMed Web of Science ®Google Scholar
• Ziegler D. M. Functional Groups bearing sulfur. Metabolic Basis of Detoxication: Metabolism of Functional Group, W. B. Jakoby, J. R. Bend, J. Caldwell. Academic Press. 1982; 171–182
   Google Scholar