A general method for affinity purification of complement component C3b using factor H-sepharose
- 1 September 1982
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 205 (3) , 575-580
- https://doi.org/10.1042/bj2050575
Abstract
Complement component C3b was 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.This publication has 26 references indexed in Scilit:
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