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Journal of Lipid Research, Vol 19, 712-722, Copyright © 1978 by Lipid Research, Inc.
K Imaizumi, M Fainaru and RJ Havel
Protein composition was determined in mesenteric lymph chylomicrons from
fat-fed rats. Among the proteins of intermediate molecular weight,
apoproteins A-I and the arginine-rich apoprotein accounted for 31% and 4%
of the total protein mass, respectively. Apoprotein B and apoprotein A-IV
each accounted for about 10% and proteins of low molecular weight (C
apoproteins and apoprotein A-II) accounted for most of the remainder.
Apoprotein A-I also accounted for more than 30% of the protein mass of
mesenteric lymph lipoproteins of density less than 1.006 g/ml ("small
chylomicrons") obtained from rats fed glucose. Aproprotein A-I was
partially dissociated from chylomicrons during brief ultracentrifugation.
Both the arginine-rich apoprotein and the C apoproteins in rat blood serum
were transferred to lymph chylomicrons from fat-fed rats during incubation
in vitro. Content of arginine-rich apoprotein, determined immunochemically,
increased six-fold when chylomicrons were diluted to a final concentration
of 500 mg/dl in blood serum. Upon incubation of chylomicrons in equivalent
volumes of ultracentrifugal fractions of serum, the increase of the
arginine-rich apoprotein was: very low density lipoproteins, 1.5-fold; high
density lipoproteins, 1.8-fold; density fraction greater than 1.006 g/ml,
5.0- fold; density fraction greater than 1.21 g/ml, 11-fold. Content of
apoprotein A-I, also determined immunochemically, was not altered
appreciably by exposure to serum or its ultracentrifugal fractions, whereas
content of C apoproteins, estimated from intensity of staining of the low
molecular weight protein component in polyacrylamide gel electropherograms,
increased in all cases except for the density fraction greater than 1.21
g/ml. The fractional content of apoprotein A- I in the protein of
chylomicrons fell after incubation, whereas that of the arginine-rich
apoprotein remained constant or rose substantially. The fractional content
of apoprotein A-IV in chylomicron-protein tended to follow that of
apoprotein A-I, as judged from polyacrylamide gel electropherograms.
Transfer of the arginine-rich and C apoproteins to chylomicrons from blood
serum was directly related to the volume of serum in which the chylomicrons
were diluted and occurred rapidly at room temperature or at 4 degrees C.
ARTICLES
Composition of proteins of mesenteric lymph chylomicrons in the rat and alterations produced upon exposure of chylomicrons to blood serum and serum proteins
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