Isolation of bovine complement factor H.

A Mhatre; W P Aston

doi:10.1016/0165-2427(87)90038-9

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PubMed · 2955562

Isolation of bovine complement factor H.

A Mhatre·W P Aston

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Abstract

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.

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Animals Cattle Chromatography, Gel Chromatography, Ion Exchange Complement C3-C5 Convertases Complement C3b Complement C3b Inactivator Proteins Complement Factor H Complement Factor I Complement Pathway, Alternative Electrophoresis, Polyacrylamide Gel Endopeptidases Hemolytic Plaque Technique Humans Journal Article Research Support, Non-U.S. Gov't

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A Mhatre, W P Aston. 1987. Isolation of bovine complement factor H.. https://doi.org/10.1016/0165-2427(87)90038-9

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