Isolation and characterization of the third component of bovine complement |
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| Authors: | Marilyn Menger WP Aston |
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| Institution: | Department of Microbiology and Immunology, Queen's University, Kingston, Ontario. K7L 3N6, Canada |
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| Abstract: | C3 was obtained from bovine serum by polyethylene glycol precipitation and chromatography on DEAE-Sephadex A-50, CM-Sephadex A-50 and Sephacryl S-200. The protein has a molecular weight of 183,000 (alpha-chain 114,000 and beta-chain 69,000). A CVF-induced bovine C3 convertase (Sepharose-CVF.Bb) cleaved C3 into C3a (11,000) and C3b (172,000) as shown by SDS-polyacrylamide gel electrophoresis. Isoelectricfocusing of C3 demonstrated at least three electrophoretic variants with pI 6.55–6.85. The isolated protein promoted the formation and action of a C3 convertase in the presence of purified bovine factors B and D. A monospecific antiserum prepared in rabbits failed to cross react with human C3 or CVF. C3c was identified as a contaminant during the isolation of C3. |
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