title: Partial purification and characterization of a peroxidase activity from human placenta.
abstract: Peroxidases can metabolize a variety of xenobiotics to reactive intermediates capable of binding to protein or DNA. The potential role of these enzymes in fetotoxicity has not been explored. In this study, the presence of peroxidase activity was observed in human term and pre-term placenta. Human term placental peroxidase activity (HTPP) was partially purified by concanavalin A affinity chromatography from CaCl2 extracts of the particulate fraction. HTPP appears to be a membrane-bound glycoprotein. Arachidonic acid-dependent oxidation of guaiacol was not observed, suggesting that the peroxidase activity was not due to prostaglandin synthase. Moreover, HTPP preparations were devoid of catalase and spectrally dissimilar from human haemoglobin, cytochrome P-450, eosinophil peroxidase and myloperoxidase, suggesting an endogenous origin. An Mr of approx. 119,000 was determined for HTPP by gel filtration. Cathodic slab-PAGE of cetyltrialkylammonium bromide-solubilized HTPP yielded two peroxidase-staining bands.
authors.affiliation: Cadmus Group Inc., Newington, VA 22122.
authors.forename: J L
authors.initials: JL
authors.lastname: Nelson
authors.forename: A P
authors.initials: AP
authors.lastname: Kulkarni
mesh_terms: D002846:Chromatography, Affinity; D005260:Female; D006801:Humans; D010544:Peroxidases / Q000302:isolation & purification* / Q000378:metabolism; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy
chemical_list: D010544:Peroxidases