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Isolation of human complement factors C3, C5 and H

Lundwall, Åke LU and Eggertsen, G. (1985) In Journal of Immunological Methods 81(1). p.60-147
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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Contribution to journal
publication status
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
Journal of Immunological Methods
volume
81
issue
1
pages
60 - 147
publisher
Elsevier
external identifiers
  • scopus:0021823952
ISSN
1872-7905
language
English
LU publication?
no
additional info
1
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
2016-04-04 13:50:37
date last changed
2021-01-03 05:24:00
@article{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.}},
  issn         = {{1872-7905}},
  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}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{60--147}},
  publisher    = {{Elsevier}},
  series       = {{Journal of Immunological Methods}},
  title        = {{Isolation of human complement factors C3, C5 and H}},
  url          = {{http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3160789}},
  volume       = {{81}},
  year         = {{1985}},
}