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- W2052646919 abstract "The lysosomal acid phosphatase (AP) and arylsulphatase (AS) activities in a tumorous blood cell line of Drosophila melanogaster have been characterized. The AP activity measured with para-nitrophenylphosphate as substrate had a pH optimum of pH 4. The Km for this substrate was 0.1 mM. The activity was inhibited by l-tartrate, fluoride ions, DFP and anions such as phosphate and molybdate, but not by sulphydryl reagents nor by alkaline phosphatase inhibitors. The activity was adsorbed onto DEAE-Sephadex at pH 8 and eluted as one peak, when a NaCl gradient was applied to the column. It was not possible to separate the activity into several components by disc-gel electrophoresis or isoelectric focusing (pI of AP: 6.2). The mobility during disc-gel electrophoresis was not altered by prior incubation with bacterial neuraminidase. The AS was shown to hydrolyse the artificial substrates para-nitrophenylsulphate, para-nitrocatecholsulphate and acetylphenyl sulphate with pH optima of 6.8–7.2. The activity was detrimentally affected by various inorganic anions and could be totally inhibited by low concentrations of AgNO3 (10−4 M). The AS bound to the anion exchanger more strongly than the AP, but in common with the AP, only one peak of activity could be detected by this and other separation techniques. The pI of the AS was 4.6. The AP and AS have similar apparent molecular weights (60–65,000) and sedimentation coefficients (6.6 and 5.8S, respectively)." @default.
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- W2052646919 date "1983-01-01" @default.
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- W2052646919 title "Characterization of the acid phosphatase and arylsulphatase activities in a tumorous blood cell line of Drosophila melanogaster" @default.
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- W2052646919 doi "https://doi.org/10.1016/0020-1790(83)90025-2" @default.
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