Some properties of ATPase activity in the intact cells of yeast Saccharomycopsis fibuligera |
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| Affiliation: | 1. Osaka University, Medical School, Nakanoshima, Kita-ku, Osaka 530, Japan;2. Osaka City Institute of Environmental Life Science, 8-34, Tojo-cho, Tennoji-ku, Osaka 543, Japan;1. MUSC Health Cystic Fibrosis Center, Medical University of South Carolina, Charleston, SC, USA;2. Quartier Bleu, Lindenhof Hospital, Bern, Switzerland;3. Centre for Experimental Medicine, Queen''s University Belfast, Belfast, UK;4. Department of Pulmonary and Critical Care Medicine, Indiana University School of Medicine, Indianapolis, IN, USA;5. Feinberg School of Medicine, Northwestern University, Chicago, IL, USA;6. Pneumologische Praxis München-Pasing, Munich, Germany;7. Pediatric Pulmonology, University Hospital of Leuven, Leuven, Belgium;8. Department of Pediatrics, Boston Children''s Hospital, Harvard Medical School, Boston, MA, USA;9. Vertex Pharmaceuticals Incorporated, Boston, MA, USA;10. ICON Clinical Research Inc, North Wales, PA, USA;11. US Food and Drug Administration, Silver Spring, MD, USA;12. Child Health Research Centre, University of Queensland, Brisbane, QLD, Australia |
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| Abstract: | - 1.1. The properties of ATPase activity were studied with the cells at the early stationary phase of Saccharomycopsis fibuligera.
- 2.2. Optimal pH for the activity was approximately 7.
- 3.3. The activity was stimulated by Mg2+.
- 4.4. The activity was inhibited by NaF, DCCD, oligomycin, NaN3, NaVO3, or PCMB but not inhibited by ouabain.
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