Isolation from human serum of an inactivator of bacterial lipopolysaccharide.
By a series of chromatographic procedures involving precipitation by salt, gel filtration, anionic exchange, and hydroxyapatite elution, a protein--termed the lipopolysaccharide inactivator (LPS-I)--has been isolated from normal human serum. As a result of treatment of bacterial lipopolysaccharide (LPS) by LPS-I, the treated LPS loses its toxicity for mice and reactivity in the Limulus assay and appears to be irreversibly disaggregated. The inactivation of the LPS by the purified LPS-I is temperature and time dependent and is not blocked by the addition of irreversible inhibitors of serine esterases. The LPS inactivator migrates as an alpha-globulin in whole serum and has a sedimentation velocity of approximately 4.5S. Characteristics of the inactivated LPS are briefly described using internally labeled LPS.
D000510:Alpha-Globulins / Q000302:isolation & purification; D000818:Animals; D001797:Blood Protein Electrophoresis; D001798:Blood Proteins / Q000302:isolation & purification*; D002850:Chromatography, Gel; D004731:Endotoxins / Q000037:antagonists & inhibitors; D006737:Horseshoe Crabs; D006801:Humans; D006882:Hydroxyapatites; D008070:Lipopolysaccharides / Q000037:antagonists & inhibitors*; D051379:Mice; D011135:Polysaccharides, Bacterial / Q000037:antagonists & inhibitors*; D013696:Temperature; D013997:Time Factors; D014461:Ultracentrifugation
D000510:Alpha-Globulins; D001798:Blood Proteins; D004731:Endotoxins; D006882:Hydroxyapatites; D008070:Lipopolysaccharides; D011135:Polysaccharides, Bacterial