Dependency of the 2,4-dinitrophenol stimulated ATPase activity on K + and respiration |
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| Authors: | A Gomez-Puyou F Sandoval M T De Gómez-Puyou A Pe?a E Chávez |
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| Affiliation: | 1. Department of Urology, China-Japan Union Hospital of Jilin University, Changchun, China;2. Department of Ultrasound, Beijing Friendship Hospital of Capital Medical University, Beijing, China;3. Department of Gastroenterology and Hepatology, China-Japan Union Hospital of Jilin University, Changchun, China;1. Key Laboratory of Coastal Environmental Processes and Ecological Remediation, Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences, Yantai, Shandong 264003, China;2. Center for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao, Shandong 266400, China;3. Qinghai Institute of Salt Lakes, Chinese Academy of Sciences, Xining, Qinghai 810008, China;1. Division of Neurobiology, Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine, Baltimore, MD, United States;2. Department of General Practice, The First hospital of China Medical University, Shenyang, Liaoning Province, China;3. Department of Pharmacology, Inner Mongolian Medical University School of Pharmacy, Hohhot, Inner Mongolian, China;4. Department of Radiology, Johns Hopkins University School of Medicine, Baltimore, MD, United States;5. Eicosanoid Core Laboratory, Division of Clinical Pharmacology, Vanderbilt University School of Medicine, Nashville, TN, United States;6. Mitochon Pharmaceuticals Inc., Radnor, PA, United States;7. Program in Cellular and Molecular Medicine, Johns Hopkins University School of Medicine, Baltimore, MD, United States;8. Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD, United States |
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| Abstract: | The 2,4-dinitrophenol (DNP) stimulated ATPase activity has been studied in rat liver mitochondria which have a K+ content of 15 mM or less. It has been found that in these mitochondria the ATPase activity becomes strictly dependent on K+ and on electron transport. The activity reaches a maximum with 20 mM KCl and is inhibited by rotenone and antimycin. Succinate, in some experiments, enhances the DNP stimulated ATPase activity in a malonate sensitive process. |
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