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- W2051205498 abstract "Subunit c of the F 1 F 0 ‐ATPase from Propionigenium modestum was extracted from the particulate cell fraction with chloroform/methanol. The protein was further purified by carboxymethyl cellulose chromatography and anion exchange HPLC in the organic solvent. SDS‐PAGE of the purified protein indicated a single stained protein band migrating as expected for the c‐subunit. Incubation of isolated subunit c in chlorform/methanol or aqueous buffer containing dodecyl‐β‐ d ‐maltoside with [ 14 C]dicyclohexylcarbodiimide (DCCD) resulted in the incorporation of radioactivity into the protein. The rate of this reaction depended on the external pH; it was significantly faster in the more acidic than in the alkaline pH range. In the presence of Na + subunit c was partially protected from labeling with [ 14 C]DCCD at pH 6.1 and at pH 7.5, whereas no protection was evident at pH 5.5. At pH 7.5, the rate of subunit c labeling by [ 14 C]DCCD in the presence of 20 mM NaCl was about 50% lower than in the absence of Na + ions. The isolated c‐subunit therefore apparently retains in part the Na + binding site which, when occupied, diminishes the reactivity of the protein towards DCCD." @default.
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- W2051205498 date "1994-03-07" @default.
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- W2051205498 title "Modification of isolated subunit c of the F<sub>1</sub>F<sub>0</sub>-ATPase from<i>Propionigenium modestum</i>by dicyclohexylcarbodiimide" @default.
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- W2051205498 doi "https://doi.org/10.1016/0014-5793(94)80147-9" @default.
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