Cross-reactive affinity purification of immunoglobulin recognizing common gram-negative bacterial core antigens

Jeff W. Tyler, James S Cullor, Jon D. Dellinger

Research output: Contribution to journalArticle

12 Scopus citations


A procedure isolating immunoglobulins specific for common gram-negative bacterial core antigens is described. A polyclonal reagent was purified by ammonium sulfate precipitation, dialysis, and column affinity chromatography. The initial vaccinal antigen was an Ra mutant Escherichia coli O111 : B4 (strain J5). The capture antigen was lipopolysaccharide derived from an Ra mutant, Salmonella typhimurium TV119 covalently-linked to an agarose matrix. Column eluants were characterized in terms of total protein concentration, IgG concentration, and EIA titer recognizing E. coli (J5). Low protein, low IgG, high EIA reading fractions were isolated, demonstrating the utility of the described technique to purify broad spectrum cross-reactive immunoglobulin reagents.

Original languageEnglish (US)
Pages (from-to)221-226
Number of pages6
JournalJournal of Immunological Methods
Issue number2
StatePublished - May 25 1990



  • Affinity chromatography
  • Gram-negative
  • Ig
  • Lipopolysaccharide

ASJC Scopus subject areas

  • Biotechnology
  • Immunology

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