Homogenates of Dunaliella primolecta, D. salina and D. tertiolecta were assayed for glycollate oxidase and glycollate dehydrogenase. Both D. primolecta and D. salina but not D. tertiolecta showed substantial glycollate-dependent O2-uptake which is characteristic of glycollate oxidase. L-Lactate was
Localization of glycollate dehydrogenase inDunaliella salina
β Scribed by A. -K. J. Sallal; R. H. Al-Hasan; N. A. Nimer
- Book ID
- 104757006
- Publisher
- Springer-Verlag
- Year
- 1987
- Tongue
- English
- Weight
- 341 KB
- Volume
- 171
- Category
- Article
- ISSN
- 0032-0935
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β¦ Synopsis
Glycollate dehydrogenase of the halotolerant green alga Dunaliella salina, isolated from a brine pond, was found associated with the membrane fraction which exhibited complete photosynthetic activity. Highest enzyme activity was found in cells grown in the presence of 5% NaCl. Any increase in NaCl concentration led to a decrease in specific enzyme activity.
π SIMILAR VOLUMES
Based on the electron-transport properties on the reducing side of the reaction center, photosystem II (PS II) in green plants and algae occurs in two distinct forms. Centers with efficient electron-transport from QA to plastoquinone (QB-reducing) account for 75% of the total PS II in the thylakoid
The occurrence of glycolate oxidase in addition to glycolate dehydrogenase in Dunaliella salina and D. primolecta, as reported in the literature, could not be confirmed. Both species were demonstrated to possess only glycolate dehydrogenase. After separation of organelles by gradient centrifugation,