Isolation and partial characterization of a fragment corresponding to the dimeric form of the CH2 domain of rabbit IgG.

A fragment corresponding to the intact dimeric form of the CH2 domain of rabbit IgG, including the hinge region disulfide linkage, was obtained by plasmin digestion of crystalline Fc derived from IgG by the action of papain. Identification and assessment of purity of the fragment was established by SDS-PAGE, amino acid composition analysis, N-terminus sequence and C-terminus amino acid analysis and SDS-urea-PAGE of the reduced fragment. The fragment retains serologic reactivity with anti-Fc specific antisera.

Assay and characterization of IgG binding to endodermal cells of the fetal rabbit yolk sac membrane.

The transfer of passive immunity in the rabbit is mediated by the fetal yolk sac membrane (YSM) and is initiated by the specific binding of IgG to receptors on the microvillar surface of the endoderm from the YSM. This report describes the preparation of suspensions of endodermal absorptive cells of the YSM and their use in equilibrium binding experiments to characterize the nature of the binding reaction. Equilibrium binding is achieved in 4 h at 4 degrees C.