Study of proteolytic removal of Fab delta and Fe delta determinants of lymphocyte membrane IgD using a direct rosette assay.

Proteolysis of lymphocyte surface membrane immunoglobulin (SIg) by trypsin, papain and pronase was investigated. Cleavage in the hinge region resulting in removal of Fab delta was distinguished from removal of the whole SIgD molecule using antisera specific for c delta l and Fc delta. Using the sensitive direct rosette assay SIgD determinants were detected after digestion under conditions previously thought to remove IgD from the membrane. By increasing digestion times is was shown that whilst papain and pronase remove the whole IgD molecule, Fc delta but not Fab delta determinants survive trypsin. The implications of the results for structural differences between membrane and serum IgD and for models of insertion of SIgD into the plasma membrane are discussed.