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• W1981695892 startingPage "925" @default.
• W1981695892 abstract "Selective carboxymethylation of disulfide bonds of the F(ab')2 fragment from rabbit IgG was performed in order to study its possible implication in the activation of the complement system by the alternative pathway. Disulfide bonds were selectively modified by reduction with different amounts of dithioerythritol (DTE)† followed by alkylation with iodoacetamide. Monovalent fragments of antibody to sheep erythrocytes, obtained after reduction and carboxymethylation, were capable of mediating the lysis of sheep erythrocytes by the alternative pathway. The chemical modification did not alter the conformational integrity of the protein as shown by CD spectra. These monovolent fragments were as efficient as the bivalent fragment when the results were normalized taking into account the loss of antibody avidity observed in the monovalent antibodies with respect to the bivalent ones. The Fab fragment, obtained by papain digestion, exhibited a similar behaviour to the Fab' fragment. This suggests that the C2-oligosaccharide present in the hinge region of the antibody molecule is not involved in the complement activation through the alternative pathway. These data may suggest that the inter-chain disulfide bonds are not involved in maintaining the effector structures required for complement activation through the alternative pathway." @default.
• W1981695892 created "2016-06-24" @default.
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• W1981695892 date "1981-10-01" @default.
• W1981695892 modified "2023-10-16" @default.
• W1981695892 title "Structural requirements of rabbit IgG F(ab')2 fragment for activation of the complement system through the alternative pathway—I. Disulfide bonds" @default.
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• W1981695892 doi "https://doi.org/10.1016/0161-5890(81)90015-8" @default.
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