A simplified method for purification of human C5a from citrated plasma

Lois Renfer, Michael M. Frank, Carl H. Hammer, Liana Harvath, Thomas J. Lawley, Kim B. Yancey

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


A simplified immunoadsorption technique has been developed to purify human C5a, the 11 000 Da glycopeptide produced by C5 convertase cleavage of the fifth component of complement. In this method, human C5 fragments, including C5a, are isolated from zymosan-activated plasma by affinity chromatography, concentrated on CM 52 cellulose, and then purified to homogeneity by gel filtration on Sephadex G-75 in phosphate-buffered saline. Human C5a prepared by this technique demonstrates characteristic immunochemical and biologic activity. This method has also been adapted for the purification of 125I-C5a in phosphate-buffered saline. This technique offers a simplified approach to the purification of this important soluble mediator of inflammation.

Original languageEnglish (US)
Pages (from-to)193-205
Number of pages13
JournalJournal of Immunological Methods
Issue number2
StatePublished - Apr 17 1986


  • Anaphylatoxin purification
  • Complement
  • Human C5a

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology


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