Scammell J G, Wear L B, Von Haven R
Department of Pharmacology, University of South Alabama College of Medicine, Mobile 36688.
Mol Cell Endocrinol. 1990 Jun 18;71(2):125-31. doi: 10.1016/0303-7207(90)90249-8.
Monoclonal antibodies generated to ovine prolactin were screened for their ability to neutralize the biological activity of prolactin from several species. By Western blot analysis, antibody 6F11 cross-reacted strongly with prolactin in homogenates of anterior pituitary glands from squirrel monkey, sheep and rat. In addition, this antibody (1 micrograms IgG/ml) completely inhibited the lactogenic activity of serum or purified prolactin (0.5 ng/ml) from rat, but not prolactin from any other source, in the Nb2 lymphoma bioassay. 6F11 cross-reacted with purified ovine and rat prolactin by enzyme-linked immunosorbentassay (ELISA) and Western blot analysis with similar affinities, suggesting that the 6F11 epitope was common to these peptides. Another monoclonal antibody (17D9, 35 ng IgG/ml) showed the opposite selectivity, completely inhibiting the activity of 0.3 ng/ml ovine prolactin, but not 0.5 ng/ml rat prolactin, in the Nb2 assay. Thus, we have identified monoclonal antibodies which cross-react with both ovine and rat prolactin, but selectively neutralize the lactogenic activity of prolactin from only one species.