Peroxidase-catalyzed displacement of tritium from regiospecifically labeled estradiol and 2-hydroxyestradiol.
Estradiol and 2-hydroxyestradiol with 3H at different positions in rings A, B or D were incubated with lactoperoxidase without added H2O2 and their oxidative transformation was followed by transfer of 3H into 3H2O. With estradiol, 3H loss from different positions in the aromatic ring was almost equal and also occurred to a lesser extent from the alicyclic portion of the molecule. Glutathione had less effect on the formation of 3H2O for the aromatic ring of estradiol than from that of the catechol estrogen where it increased the yield 6-fold. The rate of 3H loss was also very much greater from tritiated 2-hydroxyestradiol than from estradiol and NADPH was inhibitory with both steroids. Conditions for the release of 3H from estradiol and 2-hydroxyestradiol by peroxidase as well as the effect of some biochemical inhibitors were also investigated. The possible contribution of peroxidative formation of 3H2O during the radiometric assay for catechol estrogen biosynthesis by tissue monooxygenases is discussed.
Jellinck
P H
PH
Department of Biochemistry, Queen's University, Kingston, Ontario, Canada.
Bradlow
H L
HL
D004958:Estradiol / Q000031:analogs & derivatives* / Q000378:metabolism*; D002393:Estrogens, Catechol / Q000378:metabolism*; D005978:Glutathione / Q000494:pharmacology; D007784:Lactoperoxidase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D009249:NADP / Q000494:pharmacology; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D014316:Tritium
D002393:Estrogens, Catechol; D014316:Tritium; D004958:Estradiol; D009249:NADP; C001390:2-hydroxyestradiol; D007784:Lactoperoxidase; D010544:Peroxidases; D005978:Glutathione