A simplified method for purification of human C5a from citrated plasma.

Published

Journal Article

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 biological 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.

Full Text

Cited Authors

  • Renfer, L; Frank, MM; Hammer, CH; Harvath, L; Lawley, TJ; Yancey, KB

Published Date

  • April 17, 1986

Published In

Volume / Issue

  • 88 / 2

Start / End Page

  • 193 - 205

PubMed ID

  • 3514765

Pubmed Central ID

  • 3514765

International Standard Serial Number (ISSN)

  • 0022-1759

Digital Object Identifier (DOI)

  • 10.1016/0022-1759(86)90006-2

Language

  • eng

Conference Location

  • Netherlands