Purification and characterization of the soluble form of mitochondrial adenosine triphosphatase from sweet potato.
The soluble form of mitochondrial adenosine triphosphatase was purified in an electrophoretically and immunologically pure form from sweet potato root tissue. The enzyme consisted of six kinds of subunits with different molecular weights (52,500, 51,500, 35,500, 26,000, 23,000, and 12,000), and its molecular weight was about 370,000. Adenosine triphosphatase associated with the submitochondrial particles was oligomycin-sensitive and heat-labile, whereas the soluble form of the enzyme was oligomycin-insensitive and cold-labile. The enzyme in either the membrane-bound or the soluble form showed negative cooperativity. Both experiments with polyacrylamide gel electrophoresis and immunological methods suggest that some of the subunits, probably those with molecular weights of 52,500 and 51,500, are dissociated from the enzyme protein during storage of the enzyme preparations.
D000251:Adenosine Triphosphatases / Q000302:isolation & purification*; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D007120:Immunochemistry; D007425:Intracellular Membranes / Q000201:enzymology; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology*; D010944:Plants / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000302:isolation & purification; D012995:Solubility
D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases