JBC, Vol. 250, Issue 10, 3725-3728, May, 1975
Size of the polyadenylic acid region of newly synthesized globin messenger ribonucleic acid
C. G. Merkel, S. Kwan and J. B. Lingrel
The size of the polyadenylic acid region of newly synthesized globin mRNA
was determined on mRNA isolated from nucleated erythroid spleen cells of
anemic mice. The globin mRNA was purified by a combination of affinity
chromatography on oligodeoxythymidylate-cellulose (oligo-(dT)-cellulose)
and sucrose density gradient centrifugation. The purified RNA was shown to
be globin mRNA by virtue of its ability to direct the synthesis of mouse
alpha- and beta-globin chains in a cell-free system and by the presence of
two bands migrating identically with authentic mouse alpha- and beta-globin
mRNA when subjected to electrophoresis in polyacrylamide gels in the
presence of formamide. When labeled for 1 hour with [3H]adenosine, the
newly synthesized radioactive mRNA also migrated as two bands in these gels
but they moved slower than the main bands suggesting that they have higher
molecular weights. The polyadenylic acid region of the mRNA was isolated
from the T1 and pancreatic RNase digestion mixture by acrylamide sodium
dodecyl sulfate gel electrophoresis. The polyadenylic acid region was found
to contain approximately 150 adenylate residues. As it is known that globin
mRNA isolated from reticulocytes contains only 40 to 60 residues, it
follows that at least 150 adenylic acid residues are added to the globin
mRNA soon after its synthesis and that some of these are removed during the
subsequent maturation of the erythroid cell.
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