Journal of Lipid Research, Vol 27, 681-686, Copyright © 1986 by Lipid Research, Inc.
Isolation of pure LpB from human serum
R Zechner, R Moser and GM Kostner
Low density lipoproteins (LDL), even after isolation from a narrow density
cut and after several washes by preparative ultracentrifugation, are
contaminated by 3-5% non-apoB proteins. Incubation of these LDL with
artificial triglyceride-rich lipid emulsions (TGRP) removed all
contaminating apoC and also, under certain conditions, apoA proteins. TGRP
treatment did not, however, change the lipid composition and the flotation
behavior of LDL. Residual apoE and albumin, amounting up to 0.5% of the
apoB mass, were resistant to removal by TGRP treatment as well as by
heparin-Sepharose column chromatography. ApoE and albumin could only be
removed by immunoabsorption.