Abstract
Stimulation of the Escherichia coli ATPase activity by urea and trypsin shows that there is a latent ATPase activity in particles and in a crude coupling factor of E. coli. Moreover, crude coupling factor, completely dissociated by treatment with 7 M urea, can inhibit the ATPase activity of the crude coupling factor. It is suggested that the latency of the ATPase activity of the coupling factor is due to the presence of a protein, the ATPase-inhibitor.
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