[Formation of micellar complexes of apolipoprotein A-I with dimyristoylphosphatidylcholine].
Structural changes of apolipoprotein AI from human plasma high density lipoproteins in 2-chloroethanol solutions were studied using spin label and fluorescence techniques. Reversible changes in spectral parameters occur in 2-chloroethanol concentration range 0-40% and are affected by dimyristoylphosphatidylcholine, of 2-chloroethanol concentration does not exceed 30%. Dialysis experiments demonstrated the absence of binding of monomer phosphatidylcholine with apolipoprotein AI. It thus follows that formation of complexes of apolipoprotein AI with dimyristoylphosphatidylcholine is caused by lipid micella aggregation.
Misharin
A Iu
AIu
Medvedeva
N V
NV
Bushmakina
N G
NG
Antonov
I V
IV
Bushueva
T L
TL
D016632:Apolipoprotein A-I; D001054:Apolipoproteins A; D004134:Dimyristoylphosphatidylcholine; D004578:Electron Spin Resonance Spectroscopy; D005023:Ethylene Chlorohydrin; D005453:Fluorescence; D008823:Micelles; D013113:Spin Labels
D016632:Apolipoprotein A-I; D001054:Apolipoproteins A; D008823:Micelles; D013113:Spin Labels; D005023:Ethylene Chlorohydrin; D004134:Dimyristoylphosphatidylcholine
Obrazovanie mitselliarnykh kompleksov apolipoproteina A-I s dimiristoilfosfatidilkholinom.