| Abstract: | At the optimal concentrations of Mg2+ and K+ to translate total thymus PolyA+-RNA, the purified thymosin alpha 1 precursor mRNA saturate the protein synthetic activity at lower concentration than the total thymus mRNAs. The polyamine spermidine increases the translation rate of the messenger, which is modulated by magnesium, rather than improve the yield in full-length chains of thymosin alpha 1 precursor. As other eukariotic mRNAs, this messenger presents the "cap" modification at the 5'-end terminal position. The incorporation of 3H]acetate into the translation product of the messenger, shows an evidence for the acetylation of the thymosin alpha 1 precursor during its biosynthesis in vitro. |
