Abstract
AbstractThis poster presents an original technique for spreading membranes at the air/water interface.We have characterized enzymatically lipoproteins films from intestinal brush border membranes. In an attempt to study the mechanism of formation and the structure of the films obtained we used the simplest model of membrane: the liposome. Two types of films structures are formed when liposomes are spread at the air/water interface. At zero surface pressure, there is a slow transformation of the closed bilayered structure into a lipid monolayer. The internal content of the liposomes is released into the aqueous subphase. In contrast when liposomes are spread against a surface pressure they retain their internal content at the air/water interface by forming multilayered structures.We present the compression isotherms obtained by spreading intestinal brush border, erythrocyte and E. Coli cytoplasmic membranes at the air/water interface.At zero surface pressure we obtained, with a good yield, unilamellar membrane films. At high surface pressure multilamellar structures are formed. Once formed, the films are particularly stable and could be manipulated without loss of the membranous material. From doubly labelled E. Coli cytoplasmic membrane, we could show that the phospholipids and proteins spread with the same yield; as a single unit. We studied the influence of hydrolytic enzymes, chemical agents and cations on the compression isotherm of biomembranes. The changes in architecture of membrane films can provide a very simple method to study the influence of the membrane packing on the catalytic activity and protein conformation of membrane bound proteins.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call