Association of Pseudomonas cytochrome oxidase with liposomes.
Purified Pseudomonas cytochrome oxidase has been associated with asolectin liposomes by two different methods. Firstly, the enzyme was attached to liposomic membranes by adding it to a cholate-phospholipid dispersion and subsequently dialyzing the detergent out of suspension. In the second case the enzyme was adsorbed on the preformed liposomes when added to them after the dialysis. A stimulation of the cytochrome oxidase activity approximately twenty-fold was observed by the first method. In contrast, the activation was absent in the second type of preparation, indicating that interaction between the enzyme and phospholipids is very different in the two types of vesicles. The cholate-dialysis method for reconstitution of protein-phospholipid vesicles seems to lead to rather heterogenous preparations. These can be further fractionated, not only according to their size but also to the protein/phospholipid ratio, by gel chromatography.
D002499:Centrifugation, Density Gradient; D003956:Dialysis; D003576:Electron Transport Complex IV / Q000378:metabolism*; D004789:Enzyme Activation; D008081:Liposomes / Q000378:metabolism*; D008564:Membrane Potentials; D008968:Molecular Conformation; D011092:Polyethylene Glycols / Q000494:pharmacology; D011549:Pseudomonas / Q000201:enzymology
D008081:Liposomes; D011092:Polyethylene Glycols; D003576:Electron Transport Complex IV