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- W2061616402 abstract "Fifty percent of the salmon 5′-nucleotidase is in the soluble fraction after high-speed centrifugation. A threefold purification on a Sephadex G-200 column gives a specific activity of 0.5 μmoles UMP hydrolyzed per hour per milligram of protein. The pH activity curve gives a single peak with an optimum at pH 9.0 MgCl 2 , CaCl 2 , and MnSO 4 increase the activity whereas Zn acetate, Ni acetate, and CoSO 4 inhibit the enzyme. EDTA, KF 2-mercaptoethanol, and dithiothreitol inhibit the nucleotidase activity. It is stable for up to 1 week at 0 C and up to 2 hr at 35 C, but activity decreases to 50% after 15 min at 50 C and no activity is left after 15 min at 60 C. The nucleotidase shows greatest activity towards 5′-nucleotides; 2′(3′) nucleotides and 5′-deoxynucleotides are hydrolyzed less effectively. Ribose-5-phosphate and p-nitrophenylphosphate are hydrolyzed, but no activity is exhibited against fructose-1-phosphate and α-glycerophosphate." @default.
- W2061616402 created "2016-06-24" @default.
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- W2061616402 date "1970-11-01" @default.
- W2061616402 modified "2023-09-27" @default.
- W2061616402 title "5′-Nucleotidase of Testes of Immature Sockeye Salmon (Oncorhynchus nerka)" @default.
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- W2061616402 doi "https://doi.org/10.1139/f70-225" @default.
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