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- W3137602167 abstract "Alkaline phosphatase from Streptomyces hygroscopicus strain JA 5999-R 27-158 was purified and characterized. The enzyme was found in the culture filtrate and in the mycelium. The phosphatase was extracted from the mycelium and purified by adsorption to DEAE-cellulose. To separate impurities, the crude enzyme solution was heated and the phosphatase purified by chromatography through CM-Sepharose and Sephadex G 100. The specific activity of the resulting enzyme was 1000 μMol/min/mg at 25 °C. The molecular weight determined by SDS gel electrophoresis was found to be 56 000. The Michaelis-Menten constant determined with p-nitrophenylphosphate as substrate was Km = 1.25 × 10−3 M. Phosphatase activity was dependent on the presence of Ca++ and the maximum activity of enzyme with p-nitrophenylphosphate as substrate was found at pH 9.2. The pI as detected by isoelectric focusing was at pH 5.6. Temperatures from 30° to 75°C did not affect the stability of the enzyme. The alkaline phosphatase exhibited high substrate specifity; of various phosphomonoesters tested, only p-nitrophenylphosphate, methylumbelliferylphosphate, phosphoenolpyruvate, ADP, ATP and tyrosine-O-phosphate was hydrolysed. The activity was inhibited by NAF, Na2P207 and EDTA. The involvement of the alkaline phosphatase in the regulation of secondary metabolism was discussed. Es wird die Reinigung einer alkalischen Phosphatase aus Streptomyces hygroscopicus Stamm JA 5999-R 27-158 beschrieben und das gewonnene Enzym charakterisiert. Die alkalische Phosphatase kann im Kulturfiltrat wie auch im Myzel nachgewiesen werden. Sie wird vom Myzel durch alkalische Extraktion gewonnen. Aus der erhaltenen Rohenzymlösung wird die Phosphatase mittels DEAE-Celluloseadsorption, Erhitzung, CM-Sepharosechromatografie und Molekulargewichtschromatografie an Sephadex G 100 gereinigt. Das gereinigte Enzym hatte eine spezifische Aktivität von 1000 μMol/min/mg bei 25°C. Das Molekulargewicht wurde mit 56000 bestimmt. Der Km für p-Nitrophenylphosphat betrug 1,25 × 10−3 M. Die Phosphatase ist ein Ca++-abhängiges Enzym, wobei Calcium teilweise durch Magnesium oder Eisen ersetzt werden kann. Das Maximum der enzymatischen Aktivität gegenüber p-Nitrophenylphosphat liegt bei pH 9,2, der isoelektrische Punkt bei pH 5,6. Das Enzym ist bis 75 °C temperaturstabil. Es besitzt eine hohe Substratspezifität und spaltet neben p-Nitrophenylphosphat und Methylumbelliferylphosphat im wesentlichen nur Phosphoenolpyruvat, ADP, ATP und Tyrosin-O-phosphat. Die Aktivität der Phosphatase wird durch NaF, Natriumpyrophosphat und EDTA inhibiert." @default.
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- W3137602167 date "1984-12-01" @default.
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- W3137602167 title "Untersuchungen zum stoffwechsel phosphatlimitierter streptomycetenkulturen" @default.
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- W3137602167 doi "https://doi.org/10.1016/s0176-6724(84)80032-2" @default.
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