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• W2034426124 endingPage "229" @default.
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• W2034426124 abstract "The interactions of a water-soluble nonmembrane protein aprotinin with multilamellar vesicles (MLV) and small unilamellar vesicles (SUV) from soybean phospholipids were studied using Sephadex G-75 gel chromatography combined with different methods of the analysis of the eluate fractions (fluorescence, light-scattering, turbidity; 31P NMR spectroscopy). The composition of the liposomes mainly containing soybean phosphatidylcholine (PC) was varied by the addition of phosphatidylethanolamine (PE), phosphatidylinositol (PI) and lyso-phosphatidylcholine (lyso-PC). To evaluate the lipid-protein interactions, the amount of aprotinin in the MLV-aprotinin complexes was determined. Lipid-protein interactions were found to strongly depend on the liposome composition, medium pH and ionic strength. These dependencies point to the electrostatic nature of the aprotinin-lipid interactions. 31P NMR spectroscopy of the MLV-aprotinin complexes indicated that aprotinin influences the phospholipid structure in MLV at pH 3.0. In the case of PC:PE:PI and PC:PE:PI:lyso-PC vesicles, aprotinin induced liposome aggregation and a lamellar-to-isotropic phase transition of the phospholipids." @default.
• W2034426124 created "2016-06-24" @default.
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• W2034426124 date "2003-01-01" @default.
• W2034426124 modified "2023-09-27" @default.
• W2034426124 title "Interaction of the Water-Soluble Protein Aprotinin with Liposomes: Gel-Filtration, Turbidity Studies, and31P NMR Studies" @default.
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• W2034426124 doi "https://doi.org/10.1081/lpr-120026388" @default.
• W2034426124 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14670228" @default.
• W2034426124 hasPublicationYear "2003" @default.
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