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  • Title: Purification, measurement of concentration, and functional complement assay of human ficolins.
    Author: Matsushita M, Kilpatrick D, Shiraki H, Liu Y, Tateishi K, Tsujimura M, Endo Y, Fujita T.
    Journal: Methods Mol Biol; 2014; 1100():141-59. PubMed ID: 24218257.
    Abstract:
    Ficolins constitute a group of lectins involved in innate immunity. L-Ficolin, H-ficolin, and M-ficolin are present in human serum. The human ficolins differ in carbohydrate-binding specificity, but they have in common the ability to recognize the acetyl group. L-Ficolin and H-ficolin are associated with serine proteases termed MASPs (MBL-associated serine proteases) and their truncated proteins, and the complexes (L/H-ficolin-MASP) activate the lectin pathway of complement upon binding to their ligands. Recombinant M-ficolin is also able to form a complex with MASP, resulting in complement activation. L-Ficolin and H-ficolin can be purified as a complex with MASP from serum by utilizing their binding specificities. These ficolin-MASP complexes have an ability to activate C4. Human ficolins are quantified by ELISA using specific antibodies or ligands.
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