Jurtshuk, Peter, Jr.2022-06-202022-06-20197423173020https://hdl.handle.net/10657/9510The membrane-bound adenosine triphosphatase (ATPase) of Azotobacter vinelandii was examined and its direct relationship to the Azotobacter electron transport fraction (R3) was established readily. Sonically disrupted Azotobacter cells were differentially centrifuged and distribution of ATPase activity was examined in particulate and soluble fractions. Highest specific activity for ATPase was consistently found in the R3 fraction, a particulate fraction which sediments on ultracentrifugation at 144,000 x g for 2 hr. By increasing the interval time of sonication, the membrane-bound ATPase activity could not be solubilized nor released into the supernatant fraction. [...]application/pdfenThis item is protected by copyright but is made available here under a claim of fair use (17 U.S.C. Section 107) for non-profit research and educational purposes. Users of this work assume the responsibility for determining copyright status prior to reusing, publishing, or reproducing this item for purposes other than what is allowed by fair use or other copyright exemptions. Any reuse of this item in excess of fair use or other copyright exemptions requires express permission of the copyright holder.Thesisreformatted digital