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American Journal of Pathology, Vol 88, 559-574, Copyright © 1977 by American Society for Investigative Pathology

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Isolation from human serum of an inactivator of bacterial lipopolysaccharide

KJ Johnson, PA Ward, S Goralnick and MJ Osborn

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.




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Copyright © 1977 by the American Society for Investigative Pathology.