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• W1991760900 abstract "Fragmented human erythrocyte membranes were exposed to PbCl2 for 10–40 min at 23°C prior to (Na+ + K+)-ATPase assay. Inhibition increased with exposure time. Enzyme activity in 5 μg membrane protein was inhibited 50% after a 10-min exposure to 1.0 nmol PbCl2 (25 μM final concentration) and was inhibited 100% after 40 min. When membranes at various concentrations were exposed to PbCl2 for 40 min, inhibition was linear with the ratio of PbCl2 to protein. Inhibition of 100% was obtained at 0.2 nmol PbCl2/μg protein. A graph of activity vs. [protein] in the presence of PbCl2 intercepted the abscissa to the right of the origin, indicating that lead acts as an irreversible or very slowly reversible inhibitor. Addition of 1 mM 2,3-dimercaptopropanol, 1,3-dithiothreitol, dl-penicillamine or EDTA after 40 min exposure to 100 μM PbCl2 restored 45, 64, 81 and 92% of the (Na+ + K+)-ATPase, respectively. These chelators, excluding EDTA, prevented inhibition when added before PbCl2. Two washings of the membrane fragments with water or 10 mM imidazole-HCl (pH 7.4) did not restore activity. 210Pb bound tightly to membrane fragments and beginning of saturation was observed at 0.19 nmol Pb2+ bound/μg protein. This corresponded to 200 μM final concentration of PbCl2 in the ATPase assay. At 0.2 nmol PbCl2/μg protein (100% inhibition of ATPase), from 0.10–0.17 nmol of lead was bound per μg protein. Under the same conditions, 1 mM dl-penicillamine removed 80% of the bound lead which correlated with its restoration of ATPase activity. Pb2+ does not appear to denature the enzyme. The irreversible kinetics may be related to sequestration of Pb2+ within vesicles that interfere with the accessibility of chelators to Pb2+ binding sites." @default.
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• W1991760900 date "1980-07-01" @default.
• W1991760900 modified "2023-10-13" @default.
• W1991760900 title "Inhibition by lead of human erythrocyte (Na+ + K+)-adenosine triphosphatase associated with binding of 210Pb to membrane fragments" @default.
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• W1991760900 doi "https://doi.org/10.1016/0005-2736(80)90408-3" @default.
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