Abstract
Incubation of [16- 14C]oestrone with mushroom extracts or a mushroom tyrosinase preparation resulted in the formation of ether-insoluble products in high percentage yields. The nature of these metabolites has been investigated and the evidence points to an initial enzymic oxidation of oestrone to highly reactive o-quinonoid derivatives which then combine with protein or undergo alternative reactions. A very strong chemical bond is formed with protein and all attempts to release the oestrone metabolites from it were unsuccessful. Rat-liver slices are also capable of forming ether-insoluble products from oestrone, but only a relatively small fraction of these was found associated with protein. The ether-insoluble compounds showed no marked oestrogenic activity and the significance of protein binding in oestrogen metabolism is discussed.
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