Del'vig A A
Biokhimiia. 1978 Nov;43(11):1983-8.
A possible role of polynucleotide phosphorylase (PNPase) in the destruction of poly-A fragments located at the 3'-OH end of mRNA from rat liver polyribosomes was studied. Using hybridization of mRNP particles and mRNA with poly-U Sepharose 4B, it was found that polyribosomal PNPase in vitro destroys the poly-A sequences of approximately 25% of poly-A+ mRNA during the first minutes of incubation at a high rate. The destruction of the poly-A fragment of mRNA by PNPase is incomplete, since part of it is presumably protected by proteins firmly bound to the poly-A sequences of mRNA.
研究了多核苷酸磷酸化酶(PNPase)在破坏大鼠肝脏多聚核糖体mRNA 3'-OH末端的多聚A片段中的可能作用。通过将mRNP颗粒和mRNA与聚尿苷琼脂糖4B杂交发现,体外多聚核糖体PNPase在孵育的最初几分钟内以高速率破坏了约25%的多聚A+ mRNA的多聚A序列。PNPase对mRNA多聚A片段的破坏是不完全的,因为其一部分可能受到与mRNA多聚A序列紧密结合的蛋白质的保护。