Studies of the oligomycin-sensitive ATPase from yeast mitochondria. Reconstitution of ATP-32Pi exchange in the presence of phospholipids.
A purified preparation of the oligomycin-sensitive ATPase from yeast mitochondria has been shown to elicit an oligomycin- and uncoupler-senstitive ATP-32Pi exchange in the presence of phospholipids. Reconstitution was normally achieved by dialysis of an ATPase-phospholipid-cholate mixture. Following this procedure, vesicles with diameters between 200 and 1,500 A were seen by electron microscopy. As in mitochondria, ATPase activity in the reconstituted system was stimulated by a range of uncouplers which inhibited ATP-32Pi exchange. These and other findings suggest that the coupling mechanism may still be intact within the ATPase complex.
D000251:Adenosine Triphosphatases / Q000032:analysis / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000096:biosynthesis / Q000378:metabolism*; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D003486:Cyanides / Q000494:pharmacology; D008928:Mitochondria / Q000201:enzymology*; D008970:Molecular Weight; D009243:NAD / Q000494:pharmacology; D009840:Oligomycins / Q000494:pharmacology; D010101:Oxygen Consumption; D010710:Phosphates / Q000378:metabolism*; D010743:Phospholipids / Q000494:pharmacology; D012402:Rotenone / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000648:ultrastructure; D013386:Succinates / Q000494:pharmacology; D014475:Uncoupling Agents / Q000494:pharmacology
D000900:Anti-Bacterial Agents; D003486:Cyanides; D009840:Oligomycins; D010710:Phosphates; D010743:Phospholipids; D013386:Succinates; D014475:Uncoupling Agents; D012402:Rotenone; D009243:NAD; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases