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Isolation of human complement factors C3, C5 and H

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Author

Summary, in English

An improved method for simultaneous purification of complement factors C3, C5 and H from human plasma has been developed. Using an initial batch separation technique with QAE-Sephadex, followed by chromatography on SP-Sephadex and gel filtration in Sephadex G-200, 600 mg of highly pure C3 can be prepared from 1600 ml of plasma. Simultaneously about 70 mg of highly pure factor H and 30 mg of C5 are obtained by chromatography of post SP-Sephadex material on DEAE-Sephacel. A small amount of C3 in the C5 pool is removed by anti-C3-Sepharose. By maleylation or citraconylation of reduced and alkylated C3, the constitutive polypeptide chains are modified in a way that made them separable by ion exchange chromatography.

Publishing year

1985

Language

English

Pages

60-147

Publication/Series

Journal of Immunological Methods

Volume

81

Issue

1

Document type

Journal article

Publisher

Elsevier

Topic

  • Medicinal Chemistry

Keywords

  • Humans
  • Complement Factor H
  • Complement C5/*isolation & purification
  • Complement C3b Inactivator Proteins/*isolation & purification
  • Complement C3/*isolation & purification
  • Gel
  • Ion Exchange
  • Chromatography
  • Peptide Fragments/isolation & purification
  • Research Support
  • Non-U.S. Gov't

Status

Published

ISBN/ISSN/Other

  • ISSN: 1872-7905