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- W2056523432 abstract "Abstract 1. 1. A specific alkaline p -nitrophenylphosphatase ( p -nitrophenylphosphate phosphohydrolase) was purified about 200-fold from commercial baker's yeast ( Saccharomyces cerevisiae ). The enzyme was found to hydrolyse only p -nitrophenyl phosphate among several phosphomonoesters at a pH optimum of 8.0–8.2. 2. 2. The enzymatic activity was strongly increased by Mg 2+ , Ca 2+ , Zn 2+ and Be 2+ were potent inhibitors. 3. 3. EDTA decreased the enzymatic activity by lowering the concentration of Mg 2+ in the assay medium. 4. 4. Inorganic phosphate was a competitive inhibitor. 5. 5. The enzyme did not show any phosphotransferase activity when Tris was used as an acceptor. 6. 6. A molecular weight of 60 000 was estimated by gel chromatography." @default.
- W2056523432 created "2016-06-24" @default.
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- W2056523432 date "1972-05-01" @default.
- W2056523432 modified "2023-09-25" @default.
- W2056523432 title "A specific alkaline p-nitrophenylphosphatase activity from baker's yeast" @default.
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- W2056523432 doi "https://doi.org/10.1016/0005-2744(72)90338-5" @default.
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