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- W2020165324 abstract "A 5′-nucleotidase (5′-ribonucleotide phosphohydrolase, EC 3.1.3.5) from rat cerebellum was purified 855-fold by (NH4)2SO4 fractionation and column chromatography on Sephadex G-100 and G-200. The enzyme was activated by divalent cations with Mg2+, Cp2+, and Mn2+ being the most efficient activators. The 5′-nucleotidase had an optimum pH of 6.8 ± 0.2. The relative rates of hydrolysis of 5′-AMP, 5′-UMP, 5′-CMP, 5′-GMP and 5′-IMP were 100, 46, 35, 17 and 9, respectively; there was no hydrolysis of 2′- or 3′-nucleoside monophosphates. Values for the Michaelis constant were 5′-AMP, 0.08 mM; 5′-UMP, 0.82 mM; 5′-CMP, 0.92 mM; 5′-GMP, 1.41 mM; and 5′-IMP, 2.1 mM. Using 5′-AMP as substrate the 5′-nucleotidase was inhibited by NaF, HgCl2, CuCl2, p-chloromercuribenzoate, and p-hydroxymercuribenzoate. The 5′-nucleotidase was inhibited by 5 · 10−3M thymidine, guanosine and inosine but not by uridine or adenosine. The concentrations of ATP, UTP, ITP, CTP and GTP required to inhibit the hydrolysis of 5′-AMP by 50% were 10, 68, 240, 250 and 720 μM, respectively." @default.
- W2020165324 created "2016-06-24" @default.
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- W2020165324 date "1971-02-01" @default.
- W2020165324 modified "2023-10-09" @default.
- W2020165324 title "Membrane marker enzymes: Isolation, purification, and properties of 5′-nucleotidase from rat cerebellum" @default.
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- W2020165324 doi "https://doi.org/10.1016/0005-2744(71)90071-4" @default.
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