Catabolism of γG-Globulin with Reduced Interchain Disulfide Bonds in Rabbits

The interchain disulfide bonds of rabbit γG-globulin were reduced and alkylated, but the H and L polypeptide chains remained assembled due to noncovalent interactions. The in vivo degradation of these altered molecules was compared to the degradation of unaltered molecules. The plasma half-lives were found to be identical in unaltered molecules, molecules with reduced interchain disulfide bonds and molecules with reoxidized bonds. Furthermore, molecules reassembled from separated H chains labeled with I125 and L chains labeled with I131 had plasma half-life comparable to the half-life of unaltered molecules. Therefore, the integrity of interchain disulfide bonds plays no role in the biological degradation of γG-globulin molecules.