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- W2091207255 abstract "1. The biochemical characteristics of two phosphomonoesterases of the digestive canal and the hepatopancreas of a tenth instar Porcellio laevis have been studied. Enzyme activities are based on the liberation of p-nitrophenol from disodium p-nitrophenyl phosphate at 410 nm. 2. Alkaline phosphatase was found to have a linear relationship between concentration and activity, maximum activity at pH 7.79–8.10, a Michaelis constant of 3.0 × 10−4M and a temperature coefficient (Q10) of 2.25 between 20 and 30°C. 3. Barium chloride, calcium chloride, magnesium acetate and magnesium chloride acted as activators for alkaline phosphatase, while bisodium hydrogen arsenate, bisodium hydrogen phosphate, sodium arsenate and cobalt chloride inhibited the action of the enzyme. 4. Acid phosphatase has an optimum pH of 4.7, a Michaelis constant of 7.5 × 10−4M, zero-order kinetics, an optimum temperature of 50°C for a 54 min incubation period and a temperature coefficient (Q10) of 2.55 between 20 and 30°C. 5. Barium chloride, calcium chloride, magnesium acetate and magnesium chloride acted as activators for acid phosphatase, and sodium cyanide, mercuric chloride, cobalt chloride, bisodium hydrogen arsenate, bisodium hydrogen phosphate, sodium fluoride and cupric sulphate inhibited the action of the enzyme. 6. Alkaline phosphatase required 0.08M concentration of magnesium ions for its maximum activation, while acid phosphatase required 0.01M magnesium ions to attain maximum activity peak." @default.
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- W2091207255 date "1973-08-01" @default.
- W2091207255 modified "2023-09-27" @default.
- W2091207255 title "Phosphomonoesterases of the digestive gut in Porcellio laevis latreille (Porcellionidae, isopoda)" @default.
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- W2091207255 doi "https://doi.org/10.1016/0305-0491(73)90152-1" @default.
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