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  • Title: Purification and characterization of the eighth and ninth components of carp complement.
    Author: Uemura T, Yano T, Shiraishi H, Nakao M.
    Journal: Mol Immunol; 1996 Aug; 33(11-12):925-32. PubMed ID: 8960116.
    Abstract:
    Complement components corresponding to mammalian C8 and C9 were isolated from carp (Cyprinus carpio) serum. Carp C8 (M(r) 146,000) proved to be a gamma-globulin composed of three polypeptide chains (alpha-chain, M(r) 62,000; beta-chain, M(r) 62,000; gamma-chain, M(r) 22,000). The alpha-chain was disulfide-linked to the gamma-chain and the beta-chain was non-covalently associated with the alpha-gamma chain, in fair agreement with mammalian C8. However, the N-terminal amino acid sequences of the three subunits showed no homology with those of human C8. Carp C9 was an alpha-globulin composed of a single polypeptide (M(r) 91,000) and the N-terminus was blocked. Carp serum depleted of C8 did not hemolyse either carp antibody-sensitized sheep erythrocytes or non-sensitized rabbit erythrocytes, while C9-depleted carp serum did not hemolyse the former, but did hemolyse the latter target cells, as in the case of C9-depleted human serum.
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