Isolation of bovine complement factor H.
A bovine serum protein, initially recognized by its inhibitory effect on the hemolytic activity of the bovine alternative pathway was isolated from fresh bovine serum by polyethylene glycol precipitation and chromatography on DEAE-Sephacel, CM-Sephadex A-50 and Sephadex G-200. The protein, a single chain polypeptide with an apparent molecular weight of 158,000, was identified as factor H, a regulatory protein of the alternative complement pathway. Functional characterization of this protein as factor H was based on the following properties: binding to C3b, inhibition of factor B binding to C3b, cofactor activity in the cleavage of C3b by factor I, inhibition of fluid phase alternative pathway C3 convertase (C3b.Bb) formation and activity, and species-specific inhibition of the alternative pathway mediated hemolysis of heterologous erythrocytes. A monospecific rabbit antiserum against bovine factor H failed to react with human serum factor H.
D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D050577:Complement C3-C5 Convertases / Q000037:antagonists & inhibitors; D003179:Complement C3b / Q000276:immunology; D003180:Complement C3b Inactivator Proteins / Q000276:immunology / Q000302:isolation & purification*; D017242:Complement Factor H; D017244:Complement Factor I; D003170:Complement Pathway, Alternative; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000276:immunology; D006462:Hemolytic Plaque Technique; D006801:Humans
C493495:CFH protein, human; D003180:Complement C3b Inactivator Proteins; D003179:Complement C3b; D017242:Complement Factor H; D010450:Endopeptidases; D050577:Complement C3-C5 Convertases; D017244:Complement Factor I