Metabolic stability of messenger ribonucleoprotein in HeLa cells
Biochimica Et Biophysica Acta
|July 7, 1975
Abstract:
The proteins bound to HeLa cell polyribosomal messenger RNA were isolated by subjecting salt-washed, puromycin-disassembled polyribosomes to a limited digestion with pancreatic ribonuclease (ref. 1, Auerbach, S. and Pederson, T. (1975) Biochem. Biophys. Res. Commun. 63, 149-153). Label-chase experiments with radioactive amino acids revealed that the in vivo decay kinetics of the messenger RNA-associated proteins were approximately first-order, with t1/2 equal 13-15 h. The results suggest that HeLa messenger RNA and its specific set of associated proteins do not behave as single units metabolically.
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