Abstract
The soluble mitochondrial ATPase, F 1, can be slowly inactivated by incubation with Mg +2 in a manner consistent with the observations of Moyle and Mitchell ( FEBS Lett. 56 , 55 (1975)). This inhibition results in a low initial rate of ATP hydrolysis upon addition to an ATPase assay medium of F 1 which has been incubated with Mg +2. This inhibition, however, is completely reversible by Mg·ATP in a time dependent process and results in the rate of ATP hydrolysis increasing during the ATPase assay to reach control levels after 30 sec. The length of the lag is independent of the F 1 concentration in the ATPase assay and the lag is also completely reversed by subsequent incubation with excess EDTA before assay. F 1 is unstable if incubated with EDTA in the absence of free nucleotides or Mg +2. The rate of inactivation increases with decreasing protein concentration until a limiting rate is reached at high dilution. Mg +2 in excess of the EDTA or 50 μM ADP stabilize the F 1 against the inactivation but cannot reverse prior denaturation.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
