Abstract
Kinetic parameters of cleavage of CpA and UpA sites in an oligoribonucleotide under the action of artificial ribonuclease ABL3C1 were measured. The compounds were built of RNA-binding domain B, catalytic fragment C, linker L3 comprising 3 methylene groups, and aliphatic fragment A. The rate of cleavage of phosphodiester bonds in the CpA site within decaribonucleotide UUCAUGUAAA was shown to be 3.4 ± 0.2 times higher than in UpA. The rate of cleavage of phosphodiester bonds was found to depend on substrate length: a thousandfold increase in cleavage rate constant was observed for the CpA site in decaribonucleotide as compared with diribonucleoside monophosphate CpA. A slight decrease in the cleavage rates was observed for the reactions proceeding in different buffers at pH 7.0: imidazole > HEPES > phosphate > cacodylate. At the same time, the ratio of cleavage rates for CpA and UpA sites remained constant.
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Beloglazova, N.G., Mironova, N.L., Konevets, D.A. et al. Kinetic Parameters of Cleavage of CpA and UpA Sequences in an Oligoribonucleotide by Compounds Functionally Mimicking Ribonuclease A. Molecular Biology 36, 869–873 (2002). https://doi.org/10.1023/A:1021698313025
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DOI: https://doi.org/10.1023/A:1021698313025