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• W2056516326 abstract "Base-exchange activity was contrasted to the usual phosphatidohydrolase activity of commercial phospholipase D preparation from cabbage. The former activity was assayed by measuring the incorporation of labeled ethanolamine and choline into phospholipids. The latter activity was assayed by measuring the formation of phosphatidic acid with radioactive phosphatidylcholine microdispersion as substrate. The pH optimum for the base-exchange activity was about 9.0, whereas the phosphatidohydrolase activity had a pH optimum around 5.6. The incorporation of ethanolamine and choline into phospholipid was dependent upon the amount of acceptor asolectin microdispersion present. The optimum concentration of Ca2+ in the base-exchange reaction was about 4 mm, whereas the optimum concentration for the phosphatidohydrolase activity was greater than 28 mm. The incorporation of ethanolamine into phospholipid was decreased 50% by heating the enzyme preparation at 50°C for about 10 min, whereas the choline incorporation decreased approximately 20% and the phosphatidohydrolase activity decreased by about 10% under these conditions. Hemicholinium-3 was found to be a noncompetitive inhibitor for the incorporation of both ethanolamine and choline into phospholipid with respective Ki, values of 1.25 × 10−3 and 2.50 × 10−3m. The Km values for ethanolamine and choline in the base-exchange reaction were 1.25 × 10−3 and 2.50 × 10−3m, respectively. The apparent Km for phosphatidylcholine for the phosphatidohydrolase activity was about 1.5 × 10−3m, and there was no inhibition by hemicholinium-3." @default.
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• W2056516326 date "1974-10-01" @default.
• W2056516326 modified "2023-10-18" @default.
• W2056516326 title "Phosphatidohydrolase and base-exchange activity of commercial phospholipase D" @default.
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• W2056516326 doi "https://doi.org/10.1016/0003-9861(74)90051-4" @default.
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