Chicken complement factor C3 has been isolated, mapped and characterized (Laursen I & Koch C 1989; Mavrodis M et al. 1995). Chicken C3 consists of 1652 amino acids and has 54% identity with its human and mouse counterparts. Like its mammalian orthologs, chicken C3 has a two-chain structure with an alpha chain (11kDa) and a beta-chain (70kDa). Upon complement activation chicken C3 is cleaved into fragments that resemble mammalian C3a and C3b (Laursen I & Koch C 1989).
Walport, MJ, Travers, P, Shlomchik, J, Janeway C, Jr
Laursen, I, Koch, C
Mavroidis, M, Lambris, JD, Sunyer, JO
serine-type endopeptidase activity of C3 convertases [plasma membrane]
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