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Recovery of Antigenic Activity upon Reoxidation of Completely Reduced Polyalanyl Rabbit Immunoglobulin G

Murray H. Freedman 1 and Michael Sela 1

From the 1 From the Section of Chemical Immunology, The Weizmann Institute of Science, Rehovoth, Israel

Rabbit immunoglobulin G, enriched with more than 800 dl-alanine residues per molecule, still reacts with goat antibodies to immunoglobulin G. It is completely soluble in neutral aqueous buffers after total reduction (46 sulfhydryl groups per molecule) and unfolding of the molecule in 8 m guanidine hydrochloride. Following complete reduction, essentially all of the antigenic activity is lost. The recovery of antigenic activity during reoxidation is essentially independent of the protein concentration (30 to 1000 µg per ml). It is more complete at 4° than at room temperature, and, because of solubility characteristics, proceeds best with heavily alanylated preparations. Under optimal conditions of reoxidation, essentially all of the antigenic determinants can be recovered as demonstrated by precipitation with goat antibodies to immunoglobulin G, although 2.5 to 4 times more reoxidized material is required for complete precipitation of the antibodies than the corresponding untreated material. From results of experiments on reoxidation of separated chains, it seems that intrachain disulfide bonds are re-formed before the interchain disulfide bonds. The main conclusion of this paper is that it confirms the hypothesis that no genetic information other than that present in the amino acid sequence of the polypeptide chains is required for the correct conformation of a protein molecule as complex as immunoglobulin G.

Submitted on December 20, 1965


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