The partial purification of a factor from Dunaliella salina that causes the rapid in situ inactivation of light-activated chloroplast coupling factor 1 (CF1) |
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Authors: | S Selman-Reimer B R Selman |
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Affiliation: | Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison 53706. |
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Abstract: | A factor having the expected properties of the in vivo oxidant responsible for inactivating the in vivo light-activated chloroplast coupling factor 1 (CF1) has been partially purified from cell-free extracts of Dunaliella salina. This factor is highly polar, weakly acidic, and relatively temperature stable. The ability of this factor to inactivate light-activated CF1 is prevented if it is pretreated with reductants such as dithiothreitol. The factor has virtually no effect on the ethanol-induced, Mg2+ -dependent ATPase activity of the isolated CF1. |
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Keywords: | Chloroplast coupling factor 1 ATPase (Dunaliella salina) |
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