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- W2311744513 abstract "Erythrocytes contain an acid phosphomonoesterase active in varying degree with a number of phosphate ester substrates. In 1943 Behrendt observed strong activity over a pH range of 4.8 to 6.1 in human red blood cells. King and associates noted that phosphate esters of phenol were unusually active substrates, and recorded the pH of optimal activity as 4.8 to 5.2. with human material. These authors stated that no abnormalities were observed in various disease states, but did not specify the nature of disease surveyed nor the number of examples studied. In 1949 Abul-Fadl and King observed that the human erythrocytic enzyme was greatly inhibited by Cu + in concentrations as low as 0.0002 M, and that this inhibition could not be reversed by thiols. They concluded that the acid phosphatases of human erythrocytes and prostate gland were different. In 1949 Behrendt observed that the erythrocytic enzyme was 100 times more active with phenylphosphate as substrate than was the enzyme normally present in serum. Inasmuch as activity was noted with intact erythrocytes, he concluded that phenylphosphate must penetrate the membrane of the red cell, and speculated that the introduction of a phenyl group could favor lipoid solubility. Tsuboi and Hudson have extensively studied the properties of phosphomonoesterase from human red cells. With crude hemolysates," @default.
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- W2311744513 date "1961-10-01" @default.
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- W2311744513 title "Erythrocyte Acid Phosphatase in Health and Disease" @default.
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- W2311744513 doi "https://doi.org/10.1093/ajcp/36.4.328" @default.
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