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- W2018759462 abstract "Abstract 1. 1. A simple method is described for the isolation from the ribosomal ribonuclease-less strain MKE-600 of Escherichia coli of a cyclic phosphodiesterase preparation of very low endonuclease and alkaline phosphatase content. 2. 2. This enzyme is able to open cyclic phosphate ends in large fragments of TMV-RNA, but it is unable to release the resultant monoesterified phosphate in contrast to its ability to show both activities with simple model compounds. 3. 3. By the combined action of this enzyme and alkaline phosphatase (EC 3.1.3.1) all cyclic and open phosphate ends of TMV-RNA fragments appear to be dephosphorylated, as demonstrated on samples in which a limited number of breaks, calculated from infectivity loss, has been created by pancreatic ribonuclease (EC 2.7.7.16) action." @default.
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- W2018759462 date "1967-06-01" @default.
- W2018759462 modified "2023-09-23" @default.
- W2018759462 title "Action of cyclic phosphodiesterase from Escherichia coli on tobacco mosaic virus ribonucleic acid" @default.
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- W2018759462 doi "https://doi.org/10.1016/0005-2787(67)90519-9" @default.
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