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Journal of Lipid Research, Vol 30, 1525-1534, Copyright © 1989 by Lipid Research, Inc.
L Lagrost, P Gambert, M Boquillon and C Lallemant
The distribution of human apolipoprotein A-IV was studied in sera from
normolipidemic fasting subjects by high performance gel filtration on a
Superose 12 HR column. The major part of apolipoprotein A-IV eluted in the
range of the apolipoprotein A-I peak, and distributed mainly in the
large-size high density lipoprotein subfractions. Only a small peak or a
shoulder on the main fraction appeared in the elution volume of free
apolipoprotein A-IV. To investigate the relation of apolipoprotein A-IV
with high density lipoprotein particles, serum high density lipoproteins
were precipitated by incubating human serum with anti- apolipoprotein A-I
immunoglobulins. At optimal concentrations, inducing a precipitation of 90
to 95% of serum apolipoprotein A-I, about 70% of serum apolipoprotein A-IV
was precipitated. It was concluded that, in fasting human serum,
apolipoprotein A-IV was mainly associated with high density lipoprotein
particles. This high degree of association to high density lipoproteins did
not result from the known in vitro redistribution of apolipoprotein A-IV
induced by lecithin: cholesterol acyltransferase activity since it was
observed in sera in the presence of inhibitors of this enzyme. The
comparison of gel filtration profiles of total serum and of serum fractions
separated by ultracentrifugation showed that the apolipoprotein A-IV-high
density lipoprotein association was a weak one, easily dissociated by the
ultracentrifugation process. The existence in fasting human serum of a
predominant high density lipoprotein-associated form of apolipoprotein A-IV
should stimulate more studies of the general function and metabolism of
this protein.
ARTICLES
Evidence for high density lipoproteins as the major apolipoprotein A-IV- containing fraction in normal human serum
Laboratoire de Biochimie Medicale, Faculte de Medecine, Dijon, France.
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