The incorporation of acetylcholinesterase from the electric organ into liposomes.
Several methods have been used to bind electric organ aetylcholinesterase to the walls of phosphatidylcholine liposomes. One of these methods [Brunner, J., Skrabal, P. & Hauser, H. (1976) Biochim. Biophys. Acta, 455, 322-331] achieved complete incorporation, although some enzyme was shown to be sequestered inside the vesicles. The association was established either in the presence of high salt media or altered liposomal membrane fluidity. The reconstitution process impaired the allosteric transition of acetylcholinesterase which is thought to occur when Flaxedil (gallamine triethiodide) is present in a low ionic strength medium. It is suggested that the cholinesterase is capable of being incorporated into liposomes, possibly via hydrophobic forces. Such a system may be an adequate one for further study of the functioning of the enzyme in a defined membrane environment.
D000110:Acetylcholinesterase / Q000378:metabolism*; D000494:Allosteric Regulation; D000818:Animals; D003902:Detergents / Q000494:pharmacology; D004557:Electric Organ / Q000201:enzymology*; D005399:Fishes; D005703:Gallamine Triethiodide / Q000494:pharmacology; D008081:Liposomes / Q000378:metabolism*; D008297:Male; D010713:Phosphatidylcholines
D003902:Detergents; D008081:Liposomes; D010713:Phosphatidylcholines; D000110:Acetylcholinesterase; D005703:Gallamine Triethiodide