Soluble and particulate fractions from homogenates of rat uteri were capable of inactivating oxytocin and [8-lysine]-vasopressin. Little increase in the inactivating activity was noticed with extracts from pregnant as compared with nonpregnant rat uteri. An oxytocin inactivating principle from the soluble fraction was substantially purified and its action on neurohypophyseal hormones, hormonal analogs and intermediates was studied. The purified enzyme preparation was found to release glycine amide from oxytocin, deamino-oxytocin and a series of C -terminal acyclic intermediates of oxytocin; it cleaved the C-terminal glycine from oxytocinoic acid, but did not release glycine amide from [8-alanine]-oxypressin, [8-lysine]- vasopressin and [8-arginine]-vasopressin. (Endocrinology87:730,1970)
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Glass et al. (1970) studied this question.