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

From the Arthritis and Rheumatism Branch, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland

Abstract

The interchain disulfide bonds of rabbit G-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 G-globulin molecules.

Footnotes

¹ Present address: The Rockefeller University, New York, New York 10021.