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Purification and properties of heparin-releasable lipoprotein- associated
coagulation inhibitor
WF Novotny, M Palmier, TC Wun, GJ Broze and JP Miletich
Division of Hematology/Oncology, Washington University School of Medicine,
Jewish Hospital of St Louis, MO.
The lipoprotein-associated coagulation inhibitor (LACI) is present in vivo
in at least three different pools: sequestered in platelets, associated
with plasma lipoproteins, and released into plasma by intravenous heparin,
possibly from vascular endothelium. In this study we have purified the
heparin-relesable form of LACI from post-heparin plasma and show that it is
structurally different from lipoprotein LACI. The purification scheme uses
heparin-agarose chromatography, immunoaffinity chromatography, and
size-exclusion chromatography and results in a 185,000-fold purification
with a 33% yield. Heparin- releasable LACI (HRL), as analyzed by sodium
dodecyl sulfate- polyacrylamide gel electrophoresis, under reducing
conditions, appears as a major band at 40 Kd and a minor band at 36 Kd.
Immunoblot analysis suggests that the 36-Kd band arises from
carboxyl-terminus proteolysis that occurs during the purification. HRL has
a specific activity similar to that of HepG2 or lipoprotein LACI. HRL and
lipoprotein LACI combine with lipoproteins in vitro while purified HepG2
LACI does not. I125-labeled HRL, injected into a rabbit, is cleared more
slowly than I125-labeled HepG2 LACI, which may be due to attachment to
lipoproteins in vivo. Preliminary evidence suggests that HRL is associated
with vascular endothelium, possibly by attachment to glycosaminoglycans.
Volume 78,
Issue 2,
pp. 394-400,
07/15/1991
Copyright © 1991 by The American Society of Hematology
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