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. 1977 Sep;88(3):559–574.

Isolation from human serum of an inactivator of bacterial lipopolysaccharide.

K J Johnson, P A Ward, S Goralnick, M J Osborn
PMCID: PMC2032388  PMID: 70173

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)--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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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