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Recovery of Specific Activity upon Reoxidation of Completely Reduced Polyalanyl Rabbit Antibody

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

Immunospecifically purified rabbit antibodies to bovine serum albumin, enriched with more than 800 dl-alanine residues per molecule, were completely soluble in neutral aqueous buffers after total reduction (46 sulfhydryl groups per molecule) and exposure to 8 m guanidine hydrochloride. Hardly any antibody or antigenic properties could be detected in completely reduced polyalanyl antibody preparations which had been reoxidized either in the presence of 8 m urea or in 0.1 n acetic acid. Under optimum conditions of reoxidation, at least 25% of the initial antigen-combining capacity of the antibody preparations and at least 50% of their initial capacity to inhibit a homologous precipitin reaction could be recovered. These tests were used since the polyalanyl antibody preparations are unable to form macroscopic precipitates, even though they still form soluble complexes with the antigen and are capable of inhibiting the reaction of bovine serum albumin with antibodies to bovine serum albumin. The reoxidized antibody preparations exhibited a recovery of at least 68% of the antigenic determinants present in the untreated antibody molecules. The results of this investigation suggest that differences in specificity exhibited in antibody molecules are due to differences in the primary amino acid sequence of the constitutive polypeptide chains.

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