The presence of soluble carbonic anhydrase in the thylakoid lumen of chloroplasts from Arabidopsis leaves
Copyright © 2014 Elsevier GmbH. All rights reserved.
| Veröffentlicht in: | Journal of plant physiology. - 1979. - 171(2014), 11 vom: 01. Juli, Seite 903-6 |
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| Weitere Verfasser: | , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2014
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| Zugriff auf das übergeordnete Werk: | Journal of plant physiology |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Arabidopsis thaliana Carbonic anhydrase Thylakoid lumen Thylakoids Carbonic Anhydrases EC 4.2.1.1 |
| Zusammenfassung: | Copyright © 2014 Elsevier GmbH. All rights reserved. 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 β-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 |
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| Beschreibung: | Date Completed 23.01.2015 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1618-1328 |
| DOI: | 10.1016/j.jplph.2014.02.009 |