Evidence that both Ca2+-ATPase and (Ca2+ + Mg2+)-ATPase activities in the plasma membrane-rich fraction from bovine parotid gland reside on the same enzyme molecule |
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| Institution: | 1. School of Humanities and Social Sciences, Beijing Institute of Technology, Beijing 100081, China;2. CAS Key Laboratory of Behavioral Sciences, Institute of Psychology, Chinese Academy of Sciences (CAS), Beijing 100101, China;3. Department of Psychology, University of Chinese Academy of Sciences (UCAS), Beijing 100101, China;4. School of Humanities and Social Sciences, Shanxi Medical University, Shanxi 030001, China;5. Faculty of Education, the University of Hong Kong, Hong Kong;6. Department of Education, Lyuliang University, Lvliang, Shanxi 033000, China |
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| Abstract: | - 1.1. Evidence was obtained that activities of both low-affinity Ca2+-ATPase and high-affinity (Ca2+ + Mg2+)-ATPase in the plasma membrane-rich fraction from bovine parotid gland reside on the same enzyme.
- 2.2. Two solubilized ATPases were purified by four steps of HPLC; and both activities eluted at the same fractions from each column, and the specific activity ratio of the two enzymes at each step was constant.
- 3.3. By non-denaturing PAGE, the final preparation gave a single band for both protein staining and activity staining for the two ATPases; and the Ca2+-ATPase activity comigrated with that of (Ca2+ + Mg2+)-ATPase.
- 4.4. In SDS-PAGE, each activity staining for the ATPases also gave a single band, and both activities comigrated.
- 5.5. These findings suggest that Ca2+-ATPase and (Ca2+ + Mg2+)-ATPase are a single enzyme.
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