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- W63739870 abstract "Using poly(A) as a substrate, an exoribonuclease has been purified from the high-salt wash of ribosomes of Saccharomyces cerevisiae. The product of the reaction of the exoribonuclease is 5′ AMP. Hydrolysis of [3H](pA)3[14C](pA)n shows that both labels are released at the same rate, suggesting that the enzyme acts in a processive manner. Removal of the terminal phosphate of poly(A) with alkaline phosphatase reduces the rate of hydrolysis by 80%. Treatment of the terminally dephosphorylated poly(A) with polynucleotide kinase restores the activity. Two 5′ capped mRNA's have been tested and they are hydrolyzed slowly, if at all, by the enzyme. In contrast, phage T4 mRNA, ribosomal RNA, and encephalomyocarditis viral RNA are hydrolyzed at greater than 50% of the rate of poly(A)." @default.
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- W63739870 date "1978-03-01" @default.
- W63739870 modified "2023-10-11" @default.
- W63739870 title "An exoribonuclease from saccharomyces cerevisiae: Effect of modifications of 5′ end groups on the hydrolysis of substrates to 5′ mononucleotides" @default.
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- W63739870 doi "https://doi.org/10.1016/0006-291x(78)91586-3" @default.
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