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Isolation of human complement factors C3, C5 and H

Lundwall, Åke LU and Eggertsen, G. (1985) In J Immunol Methods 81(1). p.147-60
Abstract
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.
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author
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Contribution to journal
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published
subject
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
in
J Immunol Methods
volume
81
issue
1
pages
147 - 60
external identifiers
  • Scopus:0021823952
language
English
LU publication?
no
id
adee5ebd-b9a8-43f5-ab29-c3ca0102a300 (old id 3965098)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3160789
date added to LUP
2013-08-11 18:34:36
date last changed
2016-06-29 09:07:48
@misc{adee5ebd-b9a8-43f5-ab29-c3ca0102a300,
  abstract     = {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.},
  author       = {Lundwall, Åke and Eggertsen, G.},
  keyword      = {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},
  language     = {eng},
  number       = {1},
  pages        = {147--60},
  series       = {J Immunol Methods},
  title        = {Isolation of human complement factors C3, C5 and H},
  volume       = {81},
  year         = {1985},
}