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Purification and Characterization of a Glycerol-Resistant CF₀-CF₁ and CF₁-ATPase from the Halotolerant Alga Dunaliella bardawil¹

Biochemistry Department, The Weizmann Institute of Science, Rehovot 76100, Israel

The isolation of the chloroplast ATP synthase complex (CF₀-CF₁) and of CF₁ from Dunaliella bardawil is described. The subunit structure of the D. bardawil ATPase differs from that of the spinach in that the D. bardawil subunit migrates ahead of the subunit and -migrates ahead of subunit II of CF₀ when separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The CF₁ isolated from D. bardawil resembles the CF₁ isolated from Chladmydomonas reinhardi in that a reversible, Mg²⁺-dependent ATPase is induced by selected organic solvents. Glycerol stimulates cyclic photophosphorylation catalyzed by D. bardawil thylakoid membranes but inhibits photophosphorylation catalyzed by spinach thylakoid membranes. Glycerol (20%) also stimulates the rate of ATP-P_i exchange catalyzed by D. bardawil CF₀-CF₁ proteoliposomes but inhibits the activity with the spinach enzyme. The ethanol-activated, Mg²⁺-ATPase of the D. bardawil CF₁ is more resistant to glycerol inhibition than the octylglucoside-activated, Mg²⁺-ATPase of spinach CF₁ or the ethanol-activated, Mg²⁺-dependent ATPase of the C. reinhardi CF₁. Both cyclic photophosphorylation and ATP-P_i exchange catalyzed by D. bardawil CF₀-CF₁ are more sensitive to high concentrations of NaCl than is the spinach complex.

¹ Supported in part by grants from the Weizmann Institute of Science (B. R. S., Meyerhoff Fellow), the college of Agricultural and Life Sciences, University of Wisconsin (B. R. S.), the United States-Israel Binational Research Foundation (U. P. and B. R. S., BSF 2891/82), the United States-Israel Agriculture Research and Development Fund (U. P., BARD I-107-79); the United States Department of Agriculture, Science and Education Administration, CRGO (B. R. S., 82-CRCR-1-1151) and the National Institutes of Health (B. R. S., GM 31384-01).

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