Properties of univalent fragments of rabbit antibody isolated by specific adsorption

摘要: Abstract A method is described for the isolation of active nonprecipitating fragments rabbit antihapten antibody by specific adsorption. The fragments, about 1 3 as large original molecule, were isolated from a papain hydrolyzate specifically purified anti-p-azobenzoate antibody. average equilibrium constant their interaction with homologous hapten, and index heterogeneity same, within experimental error, values untreated Thus procedure does not fractionate molecules according to combining affinity. It also evident that 2 molecule may be discarded without affecting structural integrity site electrostatic effects on binding due residual bulk are negligible. number sites per determined hapten-binding measurements, 0.9–1.0, providing direct evidence produced univalent. optical rotation dialyzed approximately same γ-globulin, indicating compact molecular units; i.e., appreciably unfolded or denatured. This conclusion supported reduction in viscosity unchanged heat stability which accompanies hydrolysis.