The hydrolysis of estramustine phosphate; in vitro studies

Abstract
The ester bond by which nornitrogen mustard is linked to estradiol-17-phosphate was slowly cleaved by enzymes from the liver and prostate of the rat, dog and man. The dog tissues were more effective than those of the rat and man. Intestinal enzy-mes also exhibited the ability to hydrolyze the carbamic ester, but to a greater extent in the rat than in the dog. It is concluded that, with regard to the metabolism of estramustine, the rat is more similar to man than is the dog. Possible clinical implications of the biotransformation of estramustine phosphate are discussed.

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