The partial purification of a factor from Dunaliella salina that causes the rapid in situ inactivation of light-activated chloroplast coupling factor 1 (CF1).
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.
D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism; D000460:Chlorophyta / Q000032:analysis / Q000201:enzymology; D002736:Chloroplasts / Q000032:analysis* / Q000201:enzymology; D004229:Dithiothreitol / Q000494:pharmacology; D004789:Enzyme Activation / Q000528:radiation effects; D000431:Ethanol / Q000494:pharmacology; D008027:Light; D010084:Oxidation-Reduction; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors* / Q000378:metabolism
D000431:Ethanol; D017301:Ca(2+) Mg(2+)-ATPase; D006180:Proton-Translocating ATPases; D004229:Dithiothreitol