Complement Proteins Human Complement C5

Complement C5 is a serum glycoprotein that is cleaved to vasoactive C5a and C5b during complement activation (Morgan, 1995), and as a central component of inflammation, subsequently stimulates neutrophil-endothelial adhesion, cytokine and lipid mediator release and oxidant formation, which are associated with numerous inflammatory states and injury (Mulligan et al., 1997). An RNA library containing 2'-fluoropyrimidines were screened by SELEX for those RNA ligands that bind to human C5. After 12 rounds of selection, aptamers were identified that bound to human C5 with a Kd of 20-40 nmol/L and inhibited C5 in a human serum hemolytic activity assay (Biesecker et al., 1999).

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