title: Size and stability of dipalmitoylphosphatidylcholine/cholesterol unilamellar vesicles are affected by interaction with proteins.
abstract: The effect of entrapping the enzyme ascorbate oxidase into dipalmitoylphosphatidylcholine/cholesterol vesicles, was studied by conventional transmission electron microscopy and freeze-fracture. The freeze-fracture technique has definitely demonstrated the unilamellar nature of empty and enzyme-loaded vesicles. Images of freeze-fractured and label-fractured liposomes also indicate that the observed reduction of vesicles volume could be related to the localization of ascorbate oxidase across the membrane. The membrane localization of ascorbate oxidase may explain the oxidation of externally added ascorbate by intact enzyme-loaded liposomes. Finally, the ageing of liposomes appears to be accelerated in the presence of proteins.
authors.affiliation: Dipartimento di Biologia, Università di Roma, Tor Vergata, Italy.
authors.forename: L
authors.initials: L
authors.lastname: Dini
authors.forename: A
authors.initials: A
authors.lastname: Di Giulio
authors.forename: A
authors.initials: A
authors.lastname: Pavan
authors.forename: G
authors.initials: G
authors.lastname: Ravagnan
authors.forename: G
authors.initials: G
authors.lastname: Mossa
mesh_terms: D015060:1,2-Dipalmitoylphosphatidylcholine / Q000737:chemistry*; D001204:Ascorbate Oxidase / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D002784:Cholesterol / Q000737:chemistry*; D004795:Enzyme Stability; D005614:Freeze Fracturing; D008081:Liposomes; D008854:Microscopy, Electron; D011485:Protein Binding
chemical_list: D008081:Liposomes; D015060:1,2-Dipalmitoylphosphatidylcholine; D002784:Cholesterol; D001204:Ascorbate Oxidase