Isolation of human complement factors C3, C5 and H
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3965098
- author
- Lundwall, Åke LU and Eggertsen, G.
- publishing date
- 1985
- type
- 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}}, }