Low ionic strength or chemical cross-linking of monomeric C3b increases its binding affinity to the human complement C3b receptor.

Abstract

Quantitative studies of the interaction between a fragment of the third component of complement (C3b) and its receptor on human cells have been undertaken with a recently developed radioligand binding assay. Specific binding of fluid phase monomeric C3b was direct and saturable under low (mu = 0.0513) but not physiological (mu = 0.15) ionic strength… (More)

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@article{Arnaout1983LowIS, title={Low ionic strength or chemical cross-linking of monomeric C3b increases its binding affinity to the human complement C3b receptor.}, author={M. Amin Arnaout and Nava Dana and Jonathan Melamed and R G Medicus and Harvey R. Colten}, journal={Immunology}, year={1983}, volume={48 2}, pages={229-37} }