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- W1570863898 abstract "Abstract Several mammalian tissues have been shown to contain as many as three acid phosphatases which may be separated on the basis of differences in size by gel filtration on Sephadex G-75. The smallest of these enzymes from bovine liver, termed acid phosphatase III, has been purified to apparent homogeneity. The purified enzyme migrates as a single band during electrophoresis on polyacrylamide gel and yields arginine as the only detectable amino terminal residue. Acid phosphatase III has been characterized with respect to its substrate specificity, molecular weight, and amino acid composition. The Km value determined with p-nitrophenyl phosphate, the most readily hydrolyzed substrate tested, is 7.5 x 10-4 m. Optimal rates of hydrolysis were observed at pH 5.5. The pure enzyme is stabilized by ethylenediaminetetraacetate and phosphate ion, but is rapidly inactivated in the presence of Mg++ or mercaptoethanol. The molecular weight of acid phosphatase III determined by sedimentation equilibrium analysis is 16,590. This figure is in close agreement with the value of 16,296 obtained from the amino acid composition." @default.
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- W1570863898 date "1969-01-01" @default.
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- W1570863898 title "Purification and Characterization of a Low Molecular Weight Acid Phosphatase from Bovine Liver" @default.
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- W1570863898 doi "https://doi.org/10.1016/s0021-9258(18)94432-7" @default.
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