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PubMed · 7150233

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

J D Scott·J E Fothergill
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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.

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AnimalsCattleChromatography, AffinityChromatography, Ion ExchangeComplement C3bHumansHydrogen-Ion ConcentrationOsmolar ConcentrationProtein BindingRabbitsSepharoseJournal ArticleResearch Support, Non-U.S. Gov't

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J D Scott, J E Fothergill. 1982-09-01. A general method for affinity purification of complement component C3b using factor H-sepharose.. https://doi.org/10.1042/bj2050575

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