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- W2018177852 abstract "Inorganic phosphate has been shown to be incorporated into calf-intestinal alkaline phosphatase, since radioactive phosphorylserine could be isolated from an acid hydrolysate of a highly purified enzyme preparation, incubated with radioactive inorganic phosphate and then inactivated by acid. Much smaller amounts of labelled phosphorylserine are isolated from acetone-precipitated or heat-inactivated enzyme. After alkali inactivation of the enzyme, no phosphorylserine can be demonstrated. With a phosphate concentration of 0.03 mM, the incorporation is found to be maximal at approx. pH 5, where it is very rapid. Addition of metal ions is not necessary for the reaction. It is found that 0.01 M EDTA, 0.025 M 1-10-phenanthroline and hydrogen sulphide strongly inhibit incorporation, indicating the participation of a metal. The possible role of phosphate incorporation in the enzyme mechanism is briefly discussed." @default.
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- W2018177852 title "Studies on calf-intestinal alkaline phosphatase II. Incorporation of inorganic phosphate into a highly purified enzyme preparation" @default.
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- W2018177852 doi "https://doi.org/10.1016/0006-3002(61)90902-7" @default.
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