Purification and properties of oestrogen-induced uterine peroxidase.
1. An enzyme that can be induced in rat uteri by oestrogens and that catalyses the oxidation of guaiacol and the metabolism and binding of [4-14C]oestradiol to protein in the presence of H2O2 was partially purified by (NH4)2SO4 fractionation and polyacrylamide-gel chromatography. 2. The molecular weight of this uterine peroxidase was estimated to be about 40 000 and thus shown to differ from that of eosinophil peroxidase. 3. Cycloheximide, which blocks the increase in peroxidase activity brought about by oestrogen, was used to determine the half-life (about 4h) of the induced uterine enzyme.
D000818:Animals; D002850:Chromatography, Gel; D003513:Cycloheximide / Q000494:pharmacology; D004790:Enzyme Induction; D004958:Estradiol / Q000378:metabolism / Q000494:pharmacology*; D005260:Female; D006139:Guaiacol / Q000378:metabolism; D006207:Half-Life; D066298:In Vitro Techniques; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism; D010544:Peroxidases / Q000096:biosynthesis / Q000302:isolation & purification*; D011485:Protein Binding; D051381:Rats; D014599:Uterus / Q000187:drug effects / Q000201:enzymology*
D004958:Estradiol; D006139:Guaiacol; D003513:Cycloheximide; D010544:Peroxidases; D009247:NADH, NADPH Oxidoreductases