Abstract
IN 1955, Stotz et al.1 discovered an œstrogen-sensitive peroxidase in rat uterus and later these workers2 found that those tissues which had a high rate of cell renewal also had high peroxidase activity. This enzyme may therefore play a significant part in cell proliferation and growth, and it was thought of interest to investigate its effect on aestrogens, using initially the very stable and more readily available horseradish enzyme. In preliminary experiments3 it has already been shown that œstrone and other phenolic œstrogens could interact with protein and certain amino-acids when incubated with peroxidase under aerobic conditions, and the present communication deals with this reaction involving tryptophan.
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