Binding of ϵ-DNP-L-lysine exceeding two moles by purified chicken IgG anti-DNP antibody☆

Add time:09/07/2019    Source:sciencedirect.com

Differences in the stoichiometry of ligand binding were observed between chicken IgG and rabbit IgG anti-2,4 dinitrophenyl antibodies elicited by the same immunogen and purified by identical procedures. Equilibrium dialysis binding studies revealed the ability of chiken IgG antibody to bind more than two moles of ϵ-DNP-l-lysine ligand relative to 2 mole bound by bivalent rabbit IgG antibody. Both chicken and rabbit IgG immunoglobulins showed identical quantitative capacity to bind α,ϵ-di-DNP-l-lysine ligand. Binding of additional moles of ϵ-DNP-l-lysine by chicken antibody was shown to be specific and located in the Fab' fragments. Studies suggest that anomolous binding capacity is consistent with a larger active site in chicken IgG relative to rabbit IgG.

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