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. 1982 Nov;152(2):815–821. doi: 10.1128/jb.152.2.815-821.1982

In vitro membrane association of the F0 polypeptides of the Escherichia coli proton translocating ATPase.

K P Decker, W S Brusilow, R P Gunsalus, R D Simoni
PMCID: PMC221535  PMID: 6215396

Abstract

The F0 polypeptides a, b, and c of the H+-translocating ATPase associated with membranes when synthesized in vitro. This association occurred when the membranes were present either cotranslationally or post-translationally. In addition, the F0 polypeptides associated with liposomes. The membrane association seemed to be an insertion process since there was protection of polypeptides a and c from proteolysis. The in vitro insertion of the F0 polypeptides a, b, and c was independent of the synthesis of each polypeptide and of the F1 polypeptides.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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