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- W2010353995 abstract "The hydrogenase of Rhodopseudomonas capsulata, which is an intrinsic membrane protein, has been purified after cell breaking in a French press, extraction from the membrane by Triton X-100, precipitation by poly(ethylene glycol) 6000, chromatography on DEAE-cellulose and on hydroxyapatite and electrophoresis on polyacrylamide gel. The subunit Mr is 65000 ± 2000, and the pI 5.5. The amino acid composition is given and compared to that of other hydrogenases. Orientation of the hydrogenase protein in the membrane has been studied with the use of hydrogenase antibodies. Antibodies can reach hydrogenase in chromatophores but not in spheroplasts, indicating that the hydrogenase protein is protruding in the cytoplasmic compartment." @default.
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- W2010353995 date "1983-10-01" @default.
- W2010353995 modified "2023-10-18" @default.
- W2010353995 title "Purification, molecular properties and localization in the membrane of the hydrogenase of Rhodopseudomonas capsulata" @default.
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- W2010353995 doi "https://doi.org/10.1016/0167-4838(83)90034-1" @default.
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