Abstract
Total poly(A)-containing mRNA was isolated from rat ventral prostate and translated in a reticulocyte lysate system. The proteins corresponding to S-adenosylmethionine decarboxylase were precipitated with a specific antiserum to this protein. Two proteins were found; one having an M(r) of 32,000, which corresponded to the subunit of this enzyme, and a larger protein of M(r) 37,000. Immunopurification of polysomes with the antiserum to S-adenosylmethionine decarboxylase followed by mRNA extraction yielded an mRNA preparation which was 10-30% pure mRNA for S-adenosylmethionine decarboxylase. The translation of this mRNA showed clearly that the protein of M(r) 37,000 was a precursor of the M(r) 32,000 S-adenosylmethionine decarboxylase subunit. Treatment with 2-difluoromethylornithine, which depletes cellular spermidine and is known to increase the content of S-adenosylmethionine decarboxylase protein, led to a 9-fold increase in the content of its mRNA, but treatment with methylglyoxal bis(guanylhydrazone) did not change the mRNA content.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 13833-13837 |
| Number of pages | 5 |
| Journal | Journal of Biological Chemistry |
| Volume | 261 |
| Issue number | 29 |
| State | Published - 1986 |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology
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