Abstract
Major translation products of bovine pituitary RNA in a wheat germ cell-free system were identified as larger forms (prehormones) of growth hormone and prolactin containing amino-terminal extensions of 26 or 27 and 30 amino acid residues, respectively. However, translation of bovine pituitary RNA in the wheat germ cell-free system in the presence of microsomal membranes prepared from canine pancreas or bovine pituitary yielded products that were of the same size as authentic growth hormone and prolactin; by partial amino-terminal sequence analysis they were shown to contain the correct unique amino-terminal sequence of prolactin and the two correct amino termini of authentic growth hormone; moreover, they were found to be segregated within the microsomal vesicles in that they were largely inaccessible to degradation by proteolytic enzymes. When microsomal membranes were present after rather than during translation, prehormones were neither cleaved nor segregated. These results strongly suggest that the synthesis and segregation of the authentic hormone observed in the presence of membranes proceeds via a nascent prehormone rather than a completed prehormone.