Purification and properties of heparin-releasable lipoprotein-associated coagulation inhibitor.

摘要: The lipoprotein-associated coagulation inhibitor (LACI) is present in vivo at least three different pools: sequestered platelets, associated with plasma lipoproteins, and released into by intravenous heparin, possibly from vascular endothelium. In this study we have purified the heparin-relesable form of LACI post-heparin show that it structurally lipoprotein LACI. purification scheme uses heparin-agarose chromatography, immunoaffinity size-exclusion chromatography results a 185,000-fold 33% yield. Heparin- releasable (HRL), as analyzed sodium dodecyl sulfate- polyacrylamide gel electrophoresis, under reducing conditions, appears major band 40 Kd minor 36 Kd. Immunoblot analysis suggests 36-Kd arises carboxyl-terminus proteolysis occurs during purification. HRL has specific activity similar to HepG2 or combine lipoproteins vitro while does not. I125-labeled HRL, injected rabbit, cleared more slowly than LACI, which may be due attachment vivo. Preliminary evidence endothelium, glycosaminoglycans.