Isolation of a carp complement protein homologous to mammalian factor D
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Updated: Nov 9, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
Published on: March 9, 2010
1Laboratory of Fisheries Chemistry, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
Abstract:
Factor D of carp (Cyprinus carpio) complement was purified to apparent homogeneity by a 4-step chromatographic procedure and examined for physicochemical and functional properties. Carp factor D proved to be an alpha-globulin with a molecular mass of 29 kDa and the serum concentration was estimated to be 6 micrograms/ml. The NH2-terminal amino acid sequence (30 residues including five unidentified positions) of carp factor D showed high homologies (57-60%) to those of mammalian factor D. Neither functional compatibility nor common antigenicity was observed between carp and human factor D. This report is apparently the first description on the factor D molecule in a non-mammalian species.

