Purification of 1F5 antigen that prevents complement attack on homologous cell membranes.
Open Access
- 1 March 1990
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Immunology
- Vol. 144 (5) , 1823-1828
- https://doi.org/10.4049/jimmunol.144.5.1823
Abstract
A mAb, 1F5, has the ability to cause hemolysis by human serum of human E treated with neuraminidase via the alternative C pathway. By Western blotting, this mAb reacts with a glycoprotein having a molecular mass of 20 kDa (1F5Ag). 1F5Ag was isolated from human E by affinity chromatography with mAb-coupled Sepharose. Purified 1F5Ag was then adsorbed to guinea pig E rendering them resistant to human C attack by both the classical and the alternative pathways. Furthermore, experiments with isolated C components revealed that 1F5Ag interferes with both homologous human C8 and C9 in the terminal stage of the C reaction, whereas it has little effect on hemolysis by rabbit C8 and C9. Therefore, 1F5Ag can be called HRF20, which stands for homologous restriction factor of 20 kDa.This publication has 16 references indexed in Scilit:
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