Enzymatically deacylated lipopolysaccharide (lps) can antagonize lps at multiple sites in the lps recognition pathway (∗)

HIGHLIGHTS

• who: Richard L. Kitchens from the LPS Antagonism at Multiple Sites Jolla, CAl, and each lot was tested to determine the ratio of LBP to LPS that produced maximal binding to CD Unless otherwise stated, a molar and functional excess of LBP was used in the binding assays. On a weight basis, LBP was typically present at, fold higher concentrations than LPS. Proteinase K, phosphatidylinositol-specific phospholipase C (PI-PLC from Bacillus cereus), Nonidet, sodium deoxycholate, SDS, iodoacetamide, phenylmethylsulfonyl fluoride, aprotinin, leupeptin, TPCK, and ZPCK were obtained from Sigma. Octylglucoside (octyl-I3-D-glucopyranoside) was from Calbiochem . . .
  

   

  

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