Solubilization and further chromatographic purification of highly purified,membrane-bound Na,K-ATPase |
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| Affiliation: | 1. Institute of Physiology, Aarhus University, Aarhus, Denmark;2. Institute of Biophysics, Aarhus University, Aarhus, Denmark;1. Pharmaceutical Sciences Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran;2. Department of Toxicology, School of Pharmacy, Shahid Beheshti University of Medical Science, Tehran, Iran;3. Pharmaceutical Sciences Research Center, Shiraz University of Medical Sciences, Shiraz, Iran;4. Biochemistry Department, Tonekabon Branch, Islamic Azad University, Tonekabon, Iran;1. College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China;2. Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao 266237, China;1. School of Chemical and Biological Engineering, Seoul National University, 1, Gwanak-ro, Gwanak-gu, Seoul 08826, Republic of Korea;2. Institute of Molecular Biology and Genetics, Seoul National University, Seoul 08826, Republic of Korea;3. Interdisciplinary Program of Bioengineering, Seoul National University, Seoul 08826, Republic of Korea;4. Institute of Engineering Research, Seoul National University, Seoul 08826, Republic of Korea;5. Bio-MAX Institute, Seoul National University, Seoul 08826, Republic of Korea;6. Doping Control Center, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea |
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| Abstract: | Highly purified membrane-bound Na,K-ATPase from pig kidney outer medulla was dissolved in the non-ionic detergent C12E8. Chromatography of the dissolved material on a DEAE matrix yielded enzymatical material having a ouabain-binding capacity of 6.9 nmoles per mg protein (measured according to Lowry et al., with bovine serum albumin as standard). This material, which after addition of lipids had the same K+-phosphatase turnover as the membrane-bound enzyme, could consist entirely of live molecules with a molecular weight of 145 kDa, a value close to that expected for αβ-protomers of Na,K-ATPase. |
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