The synthesis of rat liver protein and RNA decreases with starvation. It is not yet known whether such decreases are regulated strictly at a transcriptional level, or if post-transcriptional controls are also involved. In this study we investigate the effects of 0, 2, or 4 days starvation on the levels of specific, abundant mRNAs in total and polysomal RNA populations. The mRNAs were analyzed by translation in vitro in mRNA-dependent, cell-free, protein synthesizing systems. The resulting polypeptide products were separated by gel electrophoresis and visualized with fluorography. The amount of albumin translated from both polysomal and total cellular mRNA decreased 20-40% with fasting. In contrast, a specific peptide having a molecular mass of approximately 30 kDa increased two- to three-fold in total cellular RNA with a smaller increase observed in polysomal RNA. These changes were maximal at 2 days of starvation. Since starvation is known to cause alterations in liver metabolism the 30-kDa polypeptide may be related to enzymes or other proteins involved in this homeostatic response.