Shakhov Iu A, Niren P, Baltchevski M
Biokhimiia. 1983 Aug;48(8):1347-51.
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.
采用冻融法，将从深红螺菌（R. rubrum）的载色体膜中高度纯化得到的焦磷酸酶（PPase）制剂整合到大豆磷脂脂质体中。在解偶联剂羰基氰化物-对三氟甲氧基苯腙（FCCP）、抗生素缬氨霉素（+氯化钾）和尼日利亚菌素（+氯化钾）存在的情况下，重组PPase的活性增加。寡霉素没有任何抑制作用，而亚氨二磷酸和氟化钠显著降低了整合到脂质体中的PPase的活性。在将PPase和ATP酶整合到脂质体之前对它们进行预孵育，不会影响重组酶的活性。得出的结论是，来自深红螺菌载色体的PPase整合到脂质体中时可能独立于ATP酶发挥质子泵的作用。
