Receptors for lactogenic hormones in the ovine corpus luteum. II: Specific inactivation of ovine prolactin.

Sheep corpus luteum homogenates and membrane fractions discriminate between 125I-labelled human GH (hGH) and ovine prolactin (oPRL). The present studies were designed to establish whether ovine luteal tissue possessed a prolactin-specific inactivating enzyme. Preincubation of sheep luteal microsomes and cytosol fractions with 125I-labelled hGH had little effect on the ability of the hormone to rebind to pig luteal lactogenic receptors. In contrast, sheep luteal tissue fractions markedly decreased the binding ability of 125I-labelled oPRL. However, despite the profound loss of receptor-binding activity, there was no change in protein-bound radioactivity, nor in the elution profile of 125I-labelled oPRL by gel chromatography on Sephadex G-100. Moreover, the disparity between 125I-labelled hGH and oPRL was not overcome by preincubation of sheep luteal membranes with protease inhibitors of differing specificities. We conclude that the disparity between the binding of hGH and oPRL in ovine tissues was due to the selective inactivation of oPRL. However, the activity responsible did not degrade the hormone extensively, nor was its action blocked by a range of protease inhibitors.