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Journal of Lipid Research, Vol 29, 1461-1473, Copyright © 1988 by Lipid Research, Inc.
J Elovson, JE Chatterton, GT Bell, VN Schumaker, MA Reuben, DL Puppione, JR Reeve Jr and NL Young
Rat and human very low density lipoproteins (VLDL) were fractionated by
zonal ultracentrifugation, yielding sharply defined fractions with narrow
sedimentation limits. Sedimentation coefficients for the individual
fractions were determined at two densities with the analytical
ultracentrifuge, and the results were analyzed to yield buoyant densities
and molecular weights for the particles in each fraction. For the rat
lipoproteins, the weight concentrations of triglycerides, cholesterol,
phospholipid, and protein were determined for each fraction, and their
molar concentrations of apolipoprotein B were measured with a
radioimmunoassay. For the human lipoproteins the corresponding values were
taken from Patsch et al. (Patsch, W., J. R. Patsch, G. M. Kostner, S.
Sailer, and H. Braunsteiner. 1978. Isolation of subfractions of human very
low density lipoproteins by zonal ultracentrifugation. J. Biol. Chem.
253:4911-4915). From these data, a ratio of the number of apoB peptides to
the number of lipoprotein particles was calculated for each fraction. This
ratio was close to 1 for all VLDL fractions, ranging in particle diameter
from about 40 to 80 mm and 30 to 50 mm, respectively, for rat and human
VLDL. The majority rat VLDL contain B-48 rather than B-100 as their
(single) apoB peptide. Based on these data, we proposed that only a single
copy of B- 48 is required for VLDL assembly in rat liver, unless nascent
hepatic VLDL contain additional apoB peptides which are uniformly lost from
the plasma VLDL particles when they are analyzed.
ARTICLES
Plasma very low density lipoproteins contain a single molecule of apolipoprotein B
Veterans Administration, Wadsworth Medical Service, Los Angeles, CA 90073.
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