Conformational similarity of ovine prolactin and bovine growth hormone.

The behavior and properties of ovine prolactin have been evaluated by measurements of fluorescence, polarization of fluorescence, absorption, optical rotation, and circular dichroism. The helical content of the native molecule at pH 8 is 60 per cent as determined by circular dichroism. Three molecular transitions have been followed. The one in acid affects only 20 per cent of the helical residues. More profound conformational changes occur in urea solutions (pH 5.2 and 8.0) where most of the helical residues are randomized. There is a close parallel between the behavior of ovine prolactin and bovine growth hormone both in aqueous solutions between pH 2 and 11.5 and in urea solutions at pH 5.2 and 8.0. Based on the similarities in behavior it is proposed that the conformations of these two hormones are homologous.