Carbonic Anhydrase Activity of Alkalophilic Cyanobacteria from Soda Lakes

Carbonic Anhydrase Activity of Alkalophilic Cyanobacteria from Soda Lakes The activity and intracellular partition of carbonic anhydrase (CA) were studied in alkalophilic cyanobacteria, an inhabitant of soda lakes at pH 9–10. In the homogenates of Rhabdoderma lineare, Rhabdoderma sp., and Microcoleus chthonoplastes, high activity of CA was found, similar to that in eukaryotic microalgae. The activity of CA calculated on the basis of chlorophyll and protein was higher for the soluble (sCA) than for membrane (mCA) protein fraction. Intact cells of all cyanobacteria under investigation also showed CA activity that implies the presence of extracellular form(s). The extracellular CA in benthic M. chthonoplastes was localized, at least partly, in a vast glycocalix (gCA) as shown by Western blotting and the measurement of enzyme activity in the isolated glycocalix preparations. Probing gCA from M. chthonoplastes with the antibodies against thylakoid CA from Chlamydomonas reinhardtii (Cah3) demonstrated that gCA belongs to the α-type of enzyme and has the structure identical to that of Cah3. The extracellular CA of M. chthonoplastes manifested the maximum activity at pH 7 and 10, but not at pH 6 and 9. An increase in medium pH from 7.2 to 9.6 resulted only in slight alkalization of the cytoplasm in R. lineare, from 7.1 to 7.5. It follows that true alkalophils can maintain the pH inside the cell at the near-neutral level in spite of high pH (10.2) level in the cultural medium. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Carbonic Anhydrase Activity of Alkalophilic Cyanobacteria from Soda Lakes

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Publisher
Kluwer Academic Publishers-Plenum Publishers
Copyright
Copyright © 2003 by MAIK “Nauka/Interperiodica”
Subject
Life Sciences; Plant Sciences
ISSN
1021-4437
eISSN
1608-3407
D.O.I.
10.1023/A:1024733109767
Publisher site
See Article on Publisher Site

Abstract

The activity and intracellular partition of carbonic anhydrase (CA) were studied in alkalophilic cyanobacteria, an inhabitant of soda lakes at pH 9–10. In the homogenates of Rhabdoderma lineare, Rhabdoderma sp., and Microcoleus chthonoplastes, high activity of CA was found, similar to that in eukaryotic microalgae. The activity of CA calculated on the basis of chlorophyll and protein was higher for the soluble (sCA) than for membrane (mCA) protein fraction. Intact cells of all cyanobacteria under investigation also showed CA activity that implies the presence of extracellular form(s). The extracellular CA in benthic M. chthonoplastes was localized, at least partly, in a vast glycocalix (gCA) as shown by Western blotting and the measurement of enzyme activity in the isolated glycocalix preparations. Probing gCA from M. chthonoplastes with the antibodies against thylakoid CA from Chlamydomonas reinhardtii (Cah3) demonstrated that gCA belongs to the α-type of enzyme and has the structure identical to that of Cah3. The extracellular CA of M. chthonoplastes manifested the maximum activity at pH 7 and 10, but not at pH 6 and 9. An increase in medium pH from 7.2 to 9.6 resulted only in slight alkalization of the cytoplasm in R. lineare, from 7.1 to 7.5. It follows that true alkalophils can maintain the pH inside the cell at the near-neutral level in spite of high pH (10.2) level in the cultural medium.

Journal

Russian Journal of Plant PhysiologySpringer Journals

Published: Oct 11, 2004

References

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