Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 127 - 137, Februar 1976 Human High Density Apolipoprotein A-I-Lysolecithin-Lecithin and Sphingomyelin Complexes A Method for High Yield Recombinations to Lipoprotein Complexes of Reproducible Stoichiometry Wilhelm STOFFEL and Wolfgang DARK Institut für Physiologische Chemie der Universität Köln (Received 10 December 1975) Summary: High density apolipoprotein A-I (apoLp A-I) has been prepared in a chromatographically and immunochemically homogeneous form. This apoprotein forms trimeric and tetrameric aggregates in aqueous solution at higher concentrations. ApoLp A-I has been recombined in almost quantitative yield in the presence of lysolecithin with phosphatidylcholine and sphingomyelin to particles of reproducible Stoichiometry. Lysolecithin is not required for the interactions of lecithin and sphingomyelin with the apoprotein A-I or for the stability of these complexes. Dialysis removes most of the lysolecithin without the loss of lecithin and sphingomyelin. ApoLp A-I-lecithin particles have a molecular weight of 200000 and contain 50 molecules lecithin and 25 of lysolecithin. ApoLp A-Isphingomyelin complexes contain 50 sphingomyelin and 13 lysolecithin molecules. The former particles show up as discs of 100 A diameter, and the latter particles are 250 A in diameter. Their thickness was estimated as 25 A in the apoLp A-I lecithin and 60
hoppe-seyler's zeitschrift für physiologische chemie – de Gruyter
Published: Jan 1, 1976
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