| 摘 要： | RNA ligase in eukaryotic mammalian cells was studied by using mouse brain and livercell extracts as enzyme sources and Oligo A as substrates. RNA ligase activity was deter-mined by measuring the formation of alkaline phosphate-resistant product from 5'-~32P-termi-hated Oligoribonucleotides. Under appropriate conditions, the activity of this enzyme inbrain and liver cells may vary between 16-49 mU/ml. The joining way between donorand acceptor is 5'-P→3'-OH. Further studies wore carried out by using synthetic UpCpUand ~32pNp as substrates and crude enzyme preparations from extracts of cell unclei of brainand liver as enzyme sources. RNA ligase activity was examined by homochromatographyand autoradiography. A clear joining product was demonstrated and then isolated from thereaction mixture by DEAE-Sephadex A25 column chromatography. The eluted fractionswere identified by DEAE-cellulose thin layer chromatography. The joining product washydrolyzed either with KOH or with alkaline phosphatase, the autoradiog
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