Addition of poly(A) to hnRNA in the cell nucleus is a post-transcripti
onal event and is presumed to be brought about by a specific poly(A)po
lymerase. Since it is known that tryptophan rapidly increases the cyto
plasmic levels of polyadenylated mRNA, it was of interest to investiga
te whether the essential amino acid, tryptophan, affects the enzyme re
sponsible for polyadenylation. Tryptophan (300 mg/kg body wt.) tube-fe
d 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 prote
ins separated under denaturing conditions, transferred to nitrocellulo
se sheets, and then probed with antibody raised against hepatic nuclea
r poly(A)polymerase showed no differences between the hepatic nuclei o
f control and tryptophan-treated rats.