Covalent binding of photosensitive 1-(12-azido-[9,10(-3)H2]oleoyl)glycero-3-phosphocholine (lysolecithin) to human serum high density apolipoproteins.
Human serum high density apoproteins were complexed with increasing concentrations of 1-(12-azido-[9,10(-3)H2]oleoyl)glycero-3-phosphocholine up to the saturation concentration (72 mol lysolecithin per mol apo HDL). Ultraviolet irradiation generated the nitrene which led to crosslinking with the two main apolipoproteins AI and AII. Methods are described for the removal of excess, unbound lipid and the column chromatographic separation of the lipopolypeptides AI and AII.
D001053:Apolipoproteins / Q000097:blood; D002942:Circular Dichroism; D006801:Humans; D007700:Kinetics; D008075:Lipoproteins, HDL / Q000097:blood; D008244:Lysophosphatidylcholines; D008823:Micelles; D008968:Molecular Conformation; D010782:Photolysis; D011485:Protein Binding; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence
D001053:Apolipoproteins; D008075:Lipoproteins, HDL; D008244:Lysophosphatidylcholines; D008823:Micelles