Coupling factor activity of the purified pea mitochondrial F"1-ATPase - Horak, A.; Packer, M. (Elsevier)
The pea cotyledon mitochondrial F"1-ATPase was released from the submitochondrial particles by a washing procedure using 300 mM sucrose /2 mM Tricine (pH 7.4). The enzyme was purified by DEAE-cellulose chromatography and subsequent sucrose density gradient centrifugation. Using polyacrylamide gel electrophoresis under non-denaturing conditions, the purified protein exhibited a single sharp band with slightly lower mobility than the purified pea chloroplast CF"1-ATPase. The molecular weights of pea mitochondrial F"1-ATPase and pea chloroplast CF"1-ATPase were found to be 409 000 and 378 000, respectively. The purified pea mitochondrial F"1-ATPase dissociated into six types of subunits on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Most of these subunits had mobilities different from the subunits of the pea chloroplast CF"1-ATPase. The purified mitochondrial F"1-ATPase exhibited coupling factor activity. In spite of the observed differences between CF"1 and F"1, the mitochondrial enzyme stimulated ATP formation in CF"1-depleted pea chloroplast membranes. Thus, the mitochondrial F"1 was able to substitute functionally for the chloroplast CF"1 in reconstituting photophosphorylation.
http://linkinghub.elsevier.com/retrieve/pii/0005-2728(85)90215-4
Keywords: W; V; WW-YZ; U