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Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
Published on: February 25, 2011
Effect of tryptophan on rat hepatic nuclear poly(A)polymerase activity
R N Kurl1, E Verney, H Sidransky
1Department of Pathology, The George Washington University Medical Center, 2300 Eye Street, NW, 20037, Washington, DC, USA.
Abstract:
Addition of poly(A) to hnRNA in the cell nucleus is a post-transcriptional event and is presumed to be brought about by a specific poly(A)polymerase. Since it is known that tryptophan rapidly increases the cytoplasmic levels of polyadenylated mRNA, it was of interest to investigate whether the essential amino acid, tryptophan, affects the enzyme responsible for polyadenylation. Tryptophan (300 mg/kg body wt.) tube-fed for 10 min elevated the hepatic nuclear enzymatic activities of both the chromatin-bound nuclear poly(A)polymerase (44%, n = 7) as well as that of the free solubilized form (48%, n = 7). Hepatic nuclear proteins separated under denaturing conditions, transferred to nitrocellulose sheets, and then probed with antibody raised against hepatic nuclear poly(A)polymerase showed no differences between the hepatic nuclei of control and tryptophan-treated rats.
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