ISOLATION FROM HUMAN-SERUM OF AN INACTIVATOR OF BACTERIAL LIPOPOLYSACCHARIDE

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  • 1 January 1977
    • journal article
    • research article
    • Vol. 88  (3) , 559-574
Abstract
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), was isolated from normal human serum. As a result of treatment of bacterial [Salmonella typhimurium or Escherichia coli] 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.