Receptor binding and Nb2 cell mitogenic activities of glycosylated vs. unglycosylated porcine prolactin

Purified fractions of glycosylated (pGPrl) and unglycosylated (pUGPrl) porcine prolactin were prepared by affinity chromatography on Concanavalin A-Sepharose. The relative binding activities of these two forms of prolactin for receptors from porcine mammary, adrenal cortex and rabbit mammary, as well as their Nb2 cell mitogenic activity were determined. In both the porcine mammary and adrenal cortex receptor binding assays pGPrl had a 2-3 fold lower activity than pUGPrl. In the rabbit mammary binding assay pGPrl had a about a 5 fold lower activity than pUGPrl. Similarly, pGPrl had only about 20% of the activity of pUGPrl in the Nb2 cell proliferation assay.