Isolation of human complement factors C3, C5 and H
Författare
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.
Publiceringsår
1985
Språk
Engelska
Sidor
60-147
Publikation/Tidskrift/Serie
Journal of Immunological Methods
Volym
81
Issue
1
Länkar
Dokumenttyp
Artikel i tidskrift
Förlag
Elsevier
Ämne
- Medicinal Chemistry
Nyckelord
- 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/Övrigt
- ISSN: 1872-7905