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- W2026327688 abstract "1. From a membrane fraction of bovine cerebral cotex 5′-mononucleotidase (5′-ribonucleotide phosphohydrolyase, EC 3.1.3.5) was prepared and its properties were described. 2. A particulate enzyme which was prepared by deoxycholate treatment and gradient centrifugation showed a 240-fold higher specific activity than that of the original membrane fraction. The enzyme hydrolyzed exclusively nucleoside 5′-monophosphates; and the hydrolysis rates of pyrimidine-ribose nucleotides were 2-fold larger than those of purine-ribose nucleotides. Km values for AMP and CMP were 2.9·10−4 and 4.8·10−4 M, respectively, in the presence of 2 mM MgCl2. 3. The particulate preparation was active in the absence of extraneous divalent metal ions. Both Mg2+ and Mn2+ stimulated the activity, but other tested divalent cations were inhibitory. Among nucleosides, adenosine was the most potent inhibitor regardless of the base type of the substrate. 4. Although the particulate enzyme contained phospholipids (33% of total protein), they did not seem to be involved in the activity. 5. A soluble 5′-mononucleotidase was also prepared from acetone powder of the same source, using detergent treatment and gel-filtration chromatography. The enzyme appeared to be an acidic protein possessing a strong tendency to aggregate. The apparent particle weight of the enzyme was estimated to be 190 000 by gel-filtration chromatography." @default.
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- W2026327688 date "1973-04-01" @default.
- W2026327688 modified "2023-09-24" @default.
- W2026327688 title "Isolation and properties of 5′-mononucleotidase from a membrane fraction of bovine cerebral cortex" @default.
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- W2026327688 doi "https://doi.org/10.1016/0005-2736(73)90388-x" @default.
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