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- W2000449666 abstract "Abstract 1. 1. Phosphoric ester-splitting enzymes have been obtained from defatted ragweed pollen by extraction with 0.25% sodium carbonate. The crude extract showed the presence of three optima in the pH-activity curve. After fractionation, a preparation showing two optima, one at pH 5.6 and another smaller one at 4.2 was obstained. 2. 2. The more alkaline optimum was 5.6 for sodium β-glycerophosphate, 5.7 for sodium α-glycerophosphate, and 5.5 for disodium nitrophenyl phosphate. 3. 3. On standing at pH 8.0 for 20 hr., the optimum at pH 4.2 was eliminated giving a preparation containing only one optimum. 4. 4. The Michaelis-Menten constants for the enzymatic cleavage of β-glycerophosphate and p -nitrophenyl phosphate were 3.0 × 10 −3 M and 7.5 × 10 −4 M , respectively, at the optimum pH. 5. 5. The critical inactivation temperature of the purified preparation when tested on β-glycerophosphate was observed to be 60–70 °C. 6. 6. The purified phosphatase remained stable in a milieu of pH 3–7 for a minimum period of 24 hr. at 5 °C. 7. 7. The energies of activation for the hydrolysis of β-glycerophosphate and p -nitrophenyl phosphate by the same enzyme preparation were found to be 7400 calories and 7600 calories, respectively. 8. 8. No compound was found to activate the ragweed pollen phosphatases. Copper, arsenate, cyanide, and fluoride were inhibitory to the enzyme system. 9. 9. The pollen phosphatase failed to hydrolyze a diester of ribonucleic acid, indicating the absence of diesterase and ribonuclease activities. The enzyme preparation possessed, in addition to a phosphomonoesterase activity, pyrophosphatase and adenosinetriphosphatase action." @default.
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- W2000449666 date "1951-08-01" @default.
- W2000449666 modified "2023-10-17" @default.
- W2000449666 title "Phosphatases of ragweed pollen" @default.
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- W2000449666 doi "https://doi.org/10.1016/0003-9861(51)90083-5" @default.
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