[Reconstruction of highly purified proton-translocating pyrophosphatase from Rhodospirillum rubrum].
Using the freezing-thawing procedure, a highly purified preparation of PPase from R. rubrum chromatophore membranes was incorporated into soybean phospholipid liposomes. The activity of reconstituted PPase was increased in the presence of the uncoupler, FCCP, and the antibiotics, valinomycin (+KCl) and nigericin (+KCl). Oligomycin did not exert any inhibiting action, while imidodiphosphate and NaF significantly decreased the activity of the PPase incorporated into the liposomes. Preincubation of both PPase and ATPase prior to their incorporation into the liposomes did not affect the activity of the reconstituted enzyme. It was concluded that the PPase from R. rubrum chromatophores when incorporated into the liposomes may function as a proton pump independently of the ATPase.
D005615:Freezing; D007700:Kinetics; D008081:Liposomes; D008565:Membrane Proteins / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000302:isolation & purification / Q000378:metabolism*; D012247:Rhodospirillum rubrum / Q000201:enzymology*
D008081:Liposomes; D008565:Membrane Proteins; D006180:Proton-Translocating ATPases
Rekonstruktsiia vysokoochishchennoĭ protonperenosiashcheĭ pirofosfatazy iz Rhodospirillum rubrum.