期刊
JOURNAL OF PLANT PHYSIOLOGY
卷 171, 期 11, 页码 903-906出版社
ELSEVIER GMBH
DOI: 10.1016/j.jplph.2014.02.009
关键词
Carbonic anhydrase; Arabidopsis thaliana; Thylakoids; Thylakoid lumen
资金
- CRDF Global [RUB1-2911-PU- 07]
- Russian Foundation for Basic Research [14-04-32323]
- Ministry of Education and Science of the Russian Federation [2012-1.2.2-12-000-1013-068]
Supernatant obtained after high-speed centrifugation of disrupted thylakoids that had been washed free from extrathylakoid carbonic anhydrases demonstrated carbonic anhydrase activity that was inhibited by the specific inhibitors acetazolamide and ethoxyzolamide. A distinctive feature of the effect of Triton X-100 on this activity also suggested that the source of the activity is a soluble protein. Native electrophoresis of a preparation obtained using chromatography with agarose/mafenide as an affinity sorbent revealed one protein band with carbonic anhydrase activity. The same protein was revealed in a mutant deficient in soluble stromal carbonic anhydrase beta-CA1, and this indicated that the newly revealed carbonic anhydrase is not a product of the At3g01500 gene. These data imply the presence of soluble carbonic anhydrase in the thylakoid lumen of higher plants. (C) 2014 Elsevier GmbH. All rights reserved.
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