The interaction of human apolipoprotein C-I with sub-micellar phospholipid
نویسندگان
چکیده
منابع مشابه
Visualization and analysis of apolipoprotein A-I interaction with binary phospholipid bilayers.
Apolipoprotein A-I (apoA-I) interaction with specific cell lipid domains was suggested to trigger cholesterol and phospholipid efflux. We analyzed here apoA-I interaction with dimyristoylphosphatidylcholine/distearoylphosphatidylcholine (DMPC/DSPC) bilayers at a temperature showing phase coexistence. Solid and liquid-crystalline domains were visualized by two-photon fluorescence microscopy on g...
متن کاملMicellar complexes of human apolipoprotein A-I with phosphatidylcholines and cholesterol prepared from cholate-lipid dispersions.
Micellar complexes of human apolipoprotein A-I and phosphatidylcholine, with or without cholesterol, were prepared by adding apolipoprotein A-I (apo A-I) to sodium cholate-lipid mixtures. Cholate was removed by dialysis and the apo A-I.lipid complexes were isolated by gel filtration chromatography or by density gradient ultracentrifugation. The lipid mixtures consisted of dipalmitoylphosphatidy...
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The solution properties of human plasma apolipoprotein C-II (apoC-11) have been studied by analytical ultracentrifugation, circular dichroic spectroscopy, and fluorescence spectroscopy. ApoC-Il self-associates in solution, even though no rigorous thermodynamic analysis of the mode of self-association could be established. The reversible denaturation of apoC-Il by guanidinium chloride (GdmCl) pr...
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Human plasma phospholipid transfer protein (PLTP) circulates bound to high density lipoprotein (HDL) and mediates both net transfer and exchange of phospholipids between different lipoproteins. However, its overall function in lipoprotein metabolism is unknown. To assess the effects of increased plasma levels of PLTP, human PLTP transgenic mice were established using the human PLTP gene driven ...
متن کاملHuman very low density lipoprotein structure: interaction of the C apolipoproteins with apolipoprotein B-100.
Very low density lipoproteins (VLDL) are a heterogenous population of particles differing in size and composition. Heparin-Sepharose chromatography yields three VLDL subfractions. Two subfractions, VLDLNR-1 and VLDLNR-2, which are not retained by heparin, contain little or no detectable apolipoprotein (apo)E. According to negative stain electron microscopy, VLDLNR-1 is slightly larger than VLDL...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2001
ISSN: 0014-2956
DOI: 10.1046/j.1432-1327.2001.02164.x