TY - JOUR
AU - Grossman, Arthur R.
AB - Abstract We have examined the induction of carbonic anhydrase activity in Chlamydomonas reinhardtii and have identified the polypeptide responsible for this activity. This polypeptide was not synthesized when the alga was grown photoautotrophically on 5% CO2, but its synthesis was induced under low concentrations of CO2 (air levels of CO2). In CW-15, a mutant of C. reinhardtii which lacks a cell wall, between 80 and 90% of the carbonic anhydrase activity of air-adapted cells was present in the growth medium. Furthermore, between 80 and 90% of the carbonic anhydrase is released if wild type cells are treated with autolysin, a hydrolytic enzyme responsible for cell wall degradation during mating of C. reinhardtii. These data extend the work of Kimpel, Togasaki, Miyachi (1983 Plant Cell Physiol 24: 255-259) and indicate that the bulk of the carbonic anhydrase is located either in the periplasmic space or is loosely bound to the algal cell wall. The polypeptide associated with carbonic anhydrase activity has a molecular weight of approximately 37,000. Several lines of evidence indicate that this polypeptide is responsible for carbonic anhydrase activity: (a) it appears following the transfer of C. reinhardtii from growth on 5% CO2 to growth on air levels of CO2, (b) it is located in the periplasmic space or associated with the cell wall, like the bulk of the carbonic anhydrase activity, (c) it binds dansylamide, an inhibitor of the enzyme which fluoresces upon illumination with ultraviolet light, (d) antibodies which inhibit carbonic anhydrase activity only cross-react with this 37,000 dalton species. 2 Recipient of a National Sciences and Engineering Research Council of Canada Postdoctoral Fellowship. Permanent address: University of Toronto, Botany Department, Toronto ON M5S1A1, Canada. 3 Permanent address: Indiana University, Department of Biology, Bloomington, IN 47401. 1 This research was funded by the Carnegie Institution of Washington, Publication No. 841 and National Science Foundation Grant PCM81-17958. This content is only available as a PDF. © 1984 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)
TI - Identification of Extracellular Carbonic Anhydrase of Chlamydomonas reinhardtii  
JF - Plant Physiology
DO - 10.1104/pp.76.2.472
DA - 1984-10-01
UR - https://www.deepdyve.com/lp/oxford-university-press/identification-of-extracellular-carbonic-anhydrase-of-chlamydomonas-7D9ZCYBL90
SP - 472
EP - 477
VL - 76
IS - 2
DP - DeepDyve
ER -