Abstract
Quantitative electroimmunoassays of apolipoproteins in ultracentrifugally isolated high density lipoproteins (HDL) of normolipidemic subjects showed that A-I and A-II are the major (80–85% of total HDL protein) and B, C-III, E, D and F are the minor protein constituents of this density class. A comparison between the apolipoprotein composition of ultracentrifugally isolated HDL and heparin-Mn++ supernates showed no significant difference in the levels of A-I and C-III. However, the concentration of ApoE in the heparin-Mn++ supernates was almost twice as high as that in the ultracentrifugally isolated HDL; ApoB was only detectable in trace amounts in the heparin-Mn++ supernates. To establish whether these apolipoproteins are parts of a single macromolecular complex or form separate, discrete lipoprotein particles, the high density lipoproteins were isolated by three different procedures including ultracentrifugation, heparin-Mn++ precipitation and agarose column chromatography. The double diffusion analyses of each of these HDL preparations with antisera to A-I, A-II, ApoB, C-III, ApoD, ApoE, and ApoF showed nonidentity reactions between each possible combination of these antisera. The only exception was a reaction of partial identity between antisera to A-I and A-II polypeptides indicating the occurrence of two types of lipoprotein particles, a major one (LP-A) containing both polypeptides and a minor one (LP-A-I) containing A-I as the sole protein constituent. These findings indicate that high density lipoproteins, regardless of the manner of isolation, do not consist of a single macromolecular complex, but represent a mixture of several, discrete lipoprotein families.
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Suenram, A., McConathy, W.J. & Alaupovic, P. Evidence for the lipoprotein heterogeneity of human plasma high density lipoproteins isolated by three different procedures. Lipids 14, 505–510 (1979). https://doi.org/10.1007/BF02533470
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DOI: https://doi.org/10.1007/BF02533470