Answers are grounded in this paper and cite their sources.
mRNA isolated from a line of functional rat pituitary tumor cells (GH3) added to a cell-free protein synthesizing system derived from wheat embryo directed the biosynthesis of only one protein which is immunoprecipitated by prolactin antiserum. This protein, 2000--3,000 daltons heavier than prolactin and referred to as preprolactin, appeared to represent the initial, authentic product of translation since [35S]methionine donated by initiator Met-tRNAi was documented to be incorporated into the N-terminal portion; the molar ratio of leucine: initiator methionine was estimated to be 25--28:1, while prolactin contains 22 leucine residues. The mRNA coding for preprolactin was demonstrated to migrate at approximately 12--13S using rate zonal centrifugation. These data are compatible with the postulate that preprolactin represents the intact, initial product of prolactin mRNA translation.
No takes yet. Share an insight, caveat, or question.
Evans et al. (1977) studied this question.
Synapse has enriched 5 related papers. Consider them for comparative context: