Properties of mitochondrial adenosine triphosphatase isolated from rat liver.
Soluble, oligomysin-insensitive ATPase was isolated from liver mitochondria by a new technique [Drahota and Houstĕk 1977]. Study of the resultant enzyme preparation provided further evidence that the isolated protein displays properties typical of mitochondrial ATPase (specific activity about 100 U/mg, optimum pH 8.2, activation by various bivalent cations and reassociation with membranes deprived of ATPase).
D000255:Adenosine Triphosphate / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D000818:Animals; D001639:Bicarbonates / Q000494:pharmacology; D002413:Cations, Divalent / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D008099:Liver / Q000648:ultrastructure; D008930:Mitochondria, Liver / Q000201:enzymology*; D051381:Rats
D001639:Bicarbonates; D002413:Cations, Divalent; D000255:Adenosine Triphosphate