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- W149822139 abstract "The RNA 3'-terminal phosphate cyclase catalyzes the conversion of a 3′-phosphate to a 2′,3′-phosphodiester at the end of RNA. The enzyme was discovered in HeLa cell and Xenopus oocyte nuclei extracts that were screened for the presence of RNA ligating enzymes. Conversion of the 3'-terminal phosphate in the RNA or oligoribonucleotide substrate to the 2',3'-cyclic form renders this phosphate resistant to the action of alkaline phosphatase. When 3′-terminal phosphate is the only labeled phosphate group in the RNA, generation of the phosphatase-resistant radioactivity can be conveniently measured either by trichloroacetic acid (TCA) precipitation or by retention on activated charcoal. Assays measuring the generation of phosphatase- or nuclease P1-resistant radioactivity are simple and rapid but require 3′-terminally labeled substrates. Cyclase activity, either in crude HeLa cell extracts or in the purified enzyme preparation, is highly resistant to treatment with an excess of proteases. Inclusion of protease inhibitors during purification may therefore not be necessary." @default.
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- W149822139 date "1990-01-01" @default.
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- W149822139 title "RNA 3′-terminal phosphate cyclase from HeLa cells" @default.
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- W149822139 doi "https://doi.org/10.1016/0076-6879(90)81147-m" @default.
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