Abstract
Summaryo1.An enzyme preparation which hydrolyzes TPN to DPN and inorganic phosphate has been purified from pig kidney by ammonium sulfate fractionation and trypsin digestion.2.The enzyme activity is optimal at pH 9.5 and it is activated by Mg++ and to a lesser extent by Mn++ and Ca++. Rate studies showed that the reaction was of the first order.3.A method for the determination of TPN and DPN in mixtures in a single experiment is shown.4.The enzyme preparation was not specific for TPN and hydrolyzed several phosphate esters including adenylic acids a and b. Purified preparations of alkaline phosphatase showed high TPN-dephosphorylating activity. The relationship of the TPN-dephosphorylating enzyme to alkaline phosphatase is discussed. An enzyme preparation which hydrolyzes TPN to DPN and inorganic phosphate has been purified from pig kidney by ammonium sulfate fractionation and trypsin digestion. The enzyme activity is optimal at pH 9.5 and it is activated by Mg++ and to a lesser extent by Mn++ and Ca++. Rate studies showed that the reaction was of the first order. A method for the determination of TPN and DPN in mixtures in a single experiment is shown. The enzyme preparation was not specific for TPN and hydrolyzed several phosphate esters including adenylic acids a and b. Purified preparations of alkaline phosphatase showed high TPN-dephosphorylating activity. The relationship of the TPN-dephosphorylating enzyme to alkaline phosphatase is discussed.
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