The Interaction of Lysophosphatidylcholine with Protein-Containing Liposomes1
- 1 July 1981
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 90 (3), 657-663
- https://doi.org/10.1093/oxfordjournals.jbchem.a133520
Abstract
The effect of exogenous lysophosphatidylcholine on the membranes of liposomes containing protein has been studied. Lysophosphatidylcholine severely damaged liposomes prepared in the presence of membrane proteins such as glycophorin and “band 3” protein of human erythrocytes. Some basic proteins such as cytochrome c, lysozyme and polylysine also could sensitize liposomes to lysophosphatidylcholine. As described in previous papers (Inoue, K., et al. (1974) Biochim. Biophys. Acta 363, 361-372; Utsumi, H., et al. (1978) Biochemistry17, 199–1996), large multilamellar liposomes without protein were affected by lysophosphatidylcholine only under certain conditions where a phase boundary could exist. Sonicated liposomes without protein were almost completely insensitive to lysophosphatidylcholine. Liposomes prepared by the cholate dialysis method were also insensitive to lysophosphatidylcholine, irrespective of the incubation temperature. It is known that natural membranes such as membranes of erythrocytes and of other mammalian cells are rather sensitive to lysophosphatidylcholine. The difference observed between natural membrane and liposomal membrane seems to be removed by the introduction of proteins into lipid bilayers. The mode of interaction of lysophosphatidylcholine with membranes of liposomes containing protein is discussed.Keywords
This publication has 2 references indexed in Scilit:
- Quantitative studies on lysolecithin-mediated hemolysis. Use of ether-deoxy lysolecithin analogs with varying aliphatic chain-lengthsBiochimica et Biophysica Acta (BBA) - Biomembranes, 1977
- EINE EINFACHE METHODE ZUR MIKROBESTIMMUNG VON PHOSPHAT IN DER PAPIERCHROMATOGRAPHIE1963