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PMID: 7150233 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A general method for affinity purification of complement component C3b using factor H-sepharose.

The Biochemical journal ·Vol. 205 ·No. 3 ·1982-09-01 ·Pages 575-80

Scott JD, Fothergill JE

Abstract

Complement component C3b has been purified from human, rabbit and bovine serum by affinity chromatography on human factor H-Sepharose after preliminary fractionation by poly(ethylene glycol) and DEAE-Sepharose. The yields are high (35--40%) and the whole process is rapid (3 days). Binding of C3b to factor H-Sepharose is equimolar, has a sharp optimum pH at 7.6 and is quite sensitive to ionic strength.

MeSH Terms
Animals Cattle Chromatography, Affinity/methods Chromatography, Ion Exchange Complement C3b/isolation & purification,metabolism Humans Hydrogen-Ion Concentration Osmolar Concentration Protein Binding Rabbits Sepharose
Chemicals
Complement C3b Sepharose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Scott J D
Fothergill J E
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26 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1982-09-01
Pages
575-80
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1158523
Subset
IM
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