Identification of the altered subunit in the inactive F1ATPase of an Escherichia coli uncA mutant. |
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Authors: | S D Dunn |
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Institution: | Section of Biochemistry, Molecular and Cell Biology Cornell University, Ithaca, New York 14853 USA |
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Abstract: | ATPase activity was restored to the inactive coupling factor, F1ATPase, of strain AN120 () by reconstitution of the dissociated complex with an excess of wild-type α subunit. Large excesses of α gave the highest levels of activity. The other subunits which are required for the reconstitution of ATPase activity, β and γ, did not complement the mutant enzyme. These results indicate that the α polypeptide of the AN120 ATPase is defective. |
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