Abstract
1.Propylthiouracil (PTU) was degraded by myeloperoxidase (MPO) or eosinophil peroxidase (EPO), purified from rat bone marrow, in the presence of H2O2 and Cl−. In the absence of either H2O2 or Cl−, MPO and EPO do not degrade PTU. Optimum concentrations of KCl for MPO and EPO were 50 and 250 mM, respectively.
2.The characteristics of PTU degradation by MPO-H2O2-Cl− were similar to those of the chlorinating activity of the peroxidase.
3.Hypochlorous acid as well as MPO-H2O2-Cl− also degraded PTU. Metabolites of PTU degradation by MPO-H2O2-Cl−, which were separated by C18 reversed phase h.p.l.c., were the same as those produced by hypochlorous acid.
4.Of the metabolites of PTU formed by MPO-H2O2-Cl−, one was identified as PTU sulphonic acid (6-propyl-4-hydroxypyrimidine-2-sulphonate) and another seemed to be propyluracil.