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- W2093784804 abstract "Enzymatic activity that hydrolyzes cholinephosphate and p-nitrophenyl phosphate (alkaline phosphatase, EC 3.1.3.1) has been found in two strains of HeLa cells. Both phosphatase activities were primarily associated with the microsomal fraction and had pH optima of 9–9.5. Double reciprocal plots indicated that cholinephosphate might be hydrolyzed by two distinct enzymes. p-Nitrophenyl phosphate competitively inhibited both cholinephosphate phosphatase activities. Studies with specific inhibitors suggested that both cholinephosphate phosphatase activities were the placental-type isoenzyme of alkaline phosphatase. Cholinephosphate phosphatase and p-nitrophenyl phosphate phosphatase activities comigrated on discontinuous sucrose gradients of subcellular particles. One of the strains of HeLa cells had a 500-fold higher level of cholinephosphate phosphatase than the other. The role of cholinephosphate phosphatase in phosphatidylcholine biosynthesis was investigated by comparative studies between the two strains of HeLa cells. Strain B (high level of cholinephosphate phosphatase) transported [Me-3H]choline and [Me-3H] cholinephosphate into the cells at a slightly faster rate than Strain A. Strain B incorporated radioactivity from exogenous [Me-3H]-cholinephosphate into phospholipids ten-fold faster than Strain A. However, only a 2-fold difference between the two strains was observed in the incorporation of [Me-3H]choline into the phospholipids. The activities of choline kinase (EC 2.7.1.32), cholinephosphate cytidylyltransferase (EC 2.7.7.15) and CDP-choline: 1, 2-diacylglycerol cholinephosphotransferase (EC 2.7.8.2) were similar in the two strains of HeLa cells. The data suggest that under normal growth conditions, cholinephosphate phosphatase does not influence the rate of phosphatidylcholine biosynthesis in HeLa cells." @default.
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- W2093784804 date "1977-08-01" @default.
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- W2093784804 title "The relationship between cholinephosphate phosphatase (alkaline phosphatase) and phosphatidylcholine biosynthesis in HeLa cells" @default.
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- W2093784804 doi "https://doi.org/10.1016/0005-2760(77)90175-8" @default.
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