Isolation of mouse complement component C7

J Immunol Methods. 1994 Dec 2;176(2):163-7. doi: 10.1016/0022-1759(94)90310-7.

Abstract

Mouse complement component C7 was purified from serum by a sequential procedure of fractionation precipitation by ammonium sulfate, followed by DE-52 anion exchange chromatography. Protein G affinity column chromatography, Mono S cation exchange chromatography and Superdex 200 gel filtration. The final product contained a highly purified mouse C7 component showing a single band on SDS-PAGE at the apparent Mrs of 90 kDa and 100 kDa under non-reduced and reduced conditions respectively. The yield of C7, which was measured by the biological activity, was 7.0%

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chemical Fractionation
  • Chromatography / methods
  • Complement C7 / analysis
  • Complement C7 / isolation & purification*
  • Electrophoresis, Polyacrylamide Gel
  • Mice
  • Mice, Inbred DBA

Substances

  • Complement C7