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- W2016240425 abstract "1.|ATPases are found associated with a wide variety of cell membranes. We have solubilized and purified a membrane-bound ATPase from the cyotplasmic membranes of Bacillus megaterium KM. 2.|The properties of the membrane bound and solubilized enzyme are similar. It is activated by both Ca2+ and Mg2+, but preferentially by Ca2+. It is slowly inactivated at 4°. In addition to ATP it can use GTP and ITP as substrates. It is competitively inhibited by ADP. 3.|The solubilized ATPase binds back to membranes depleted of ATPase, in the presence of 0.01 M Ca2+. It does not bind to undepleted membranes. 4.|The enzyme is released from the membrane by washing with 0.003 M Tris-HCl (pH 7.5). It is further purified by absorption on DEAE-cellulose, followed by elution with (NH4)2SO4. On polyacrylamide gel electrophoresis at pH 8.8 and pH 8.0, the purified enzyme appears as a major band which has ATPase activity. On polyacrylamide gel electrophoresis in 0.1 % sodium dodecyl sulfate, the protein is inactivated and one major band of molecular weight approx. 69 000 is seen. Since the active protein is excluded from Sephadex G-100 gel, its molecular weight must be greater than 100 000, suggesting that the band seen on polyacrylamide gel electrophoresis in sodium dodecyl sulfate must represent subunits of the whole protein." @default.
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- W2016240425 date "1971-09-01" @default.
- W2016240425 modified "2023-09-23" @default.
- W2016240425 title "Purification and properties of ATPase from the cytoplasmic membrane of Bacillus megaterium KM" @default.
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- W2016240425 doi "https://doi.org/10.1016/0005-2736(71)90011-3" @default.
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