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- W2029126612 abstract "1. A new nucleotidase (nucleotide phosphohydrolase) unique in its high activity toward deoxyribonucleotides, has been purified approximately 2000-fold from the 123 000 × g supernatant of rat liver homogenate. 2. The enzyme hydrolyzed deoxythymidine 3′,5′-diphosphate more rapidly than the 5′-monophosphates of deoxythymidine, deoxyuridine, and deoxyguanosine, which were degraded at similar rates. Other 5′-nucleotides were only slightly or insignificantly degraded. The enzyme also possessed 3′-nucleotidase activity and hydrolyzed, in decreasing order of effectiveness, the 3′-monophosphate of deoxythymidine, uridine and guanosine. Other 3′-ribonucleotides were inactive as substrates. p-Nitrophenyl phosphate was dephosphorylated to a certain extent. 3. The pH optimum of the enzyme varied within the range of 5.6–6.4 depending on the substrate used. The enzyme was Mg2+ dependent, contained an essential SH group(s), and was moderately stable. It had a molecular weight of about 45 000. The apparent Km values, which were higher for the 5′-nucleotides than for the 3′-isomers, ranged from 1.1 mM to 0.16 mM. 4. Identity of the 5′- and 3′-nucleotidase and the p-nitrophenyl phosphatase activities with a single protein was supported by the constant ratio of the activities during purification, parallel loss of activities upon storage, and elution of the activities in a single peak from both DEAE-Sephadex and Sephadex G-100 columns. 5. The enzyme activity with varied combinations of two different nucleotides indicated that the enzyme may possess either two catalytic sites hydrolyzing 5′- and 3′-nucleotides, respectively, or an allosteric site at which one of the nucleotides can bind and activate the dephosphorylation of the other." @default.
- W2029126612 created "2016-06-24" @default.
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- W2029126612 date "1971-04-01" @default.
- W2029126612 modified "2023-09-27" @default.
- W2029126612 title "A new nucleotidase of rat liver with activity toward 3′- and 5′-nucleotides" @default.
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- W2029126612 doi "https://doi.org/10.1016/0005-2744(71)90040-4" @default.
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