[Detergent properties of apolipoprotein A1 in micellar complexes with dimyristoyl phosphatidylcholine].
Bilayer micellar complexes of the human plasma apolipoprotein A1 with dimyristoyl phosphatidylcholine were prepared under kinetically controlled conditions. Detergent-like properties of Apo A1 in the complexes were expressed in terms of delta SA1 parameter (surface area of mixed micelle per an Apo A1 molecule). Analysis of our and earlier published data showed the correlation of the delta SA1 parameter with the stoichiometry of complexes. Changes of detergent-like properties were caused by cross-linking or proteolysis of Apo A1.
Misharin
A Iu
AIu
Zamaeva
N Iu
NIu
Antonov
I V
IV
Bushmakina
N G
NG
Medvedeva
N V
NV
D016632:Apolipoprotein A-I; D001054:Apolipoproteins A; D002853:Chromatography, Liquid; D003432:Cross-Linking Reagents; D003902:Detergents; D004134:Dimyristoylphosphatidylcholine; D006801:Humans; D006868:Hydrolysis; D008051:Lipid Bilayers; D008075:Lipoproteins, HDL; D008823:Micelles; D008854:Microscopy, Electron; D013501:Surface-Active Agents
D016632:Apolipoprotein A-I; D001054:Apolipoproteins A; D003432:Cross-Linking Reagents; D003902:Detergents; D008051:Lipid Bilayers; D008075:Lipoproteins, HDL; D008823:Micelles; D013501:Surface-Active Agents; D004134:Dimyristoylphosphatidylcholine
Detergentnye svoĭstva apolipoproteina A1 v mitselliarnykh kompleksakhs dimiristoilfosfatidilkholinom.