[Studies on the activity of aldolase from rabbit muscles in the presence of liposomes].
Electronmicroscopic studies have been made on the structure of liposomes obtained by the method of Bangham [13] with subsequent ultrasonic desintegration. The effect of muscle aldolase on the structure of liposomes was also investigated. Parallel studies were made on the effect of storage of liposomes upon the activity of aldolase. It was shown that liposomes obtained from chromatographically pure egg lecithin present discrete partially aggregated bodies, 1.000-3.000 A in size, composed by concentric layers, which have a dimension of approximately 40 A and periodicity of about 70 A. Interaction of these particles with the protein results into their desintegration and enlargement, this process being accompanied by the formation of a "fringe" at the edge of the particles. Aldolase activity in these systems in higher than in control. During storage of phosphatide-aqueous system, obtained by the metod of Bungenberg de Jong, activation of aldolase is gradually replaced by its inactivation.
D000818:Animals; D001665:Binding Sites; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D007700:Kinetics; D008081:Liposomes / Q000494:pharmacology*; D008968:Molecular Conformation; D009132:Muscles / Q000187:drug effects / Q000201:enzymology*; D010713:Phosphatidylcholines; D011817:Rabbits
D008081:Liposomes; D010713:Phosphatidylcholines; D005634:Fructose-Bisphosphate Aldolase
Izuchenie aktivnosti al'dolazy iz m'shts krolika v prisutstvii liposom