Abstract
An allergenically active protein isolated from cod white muscle albumin and designated DS 22 was subjected to denaturation experiments by 8M urea/β-mercaptoethanol and high concentrations of guanidine hydrochloride. The allergenic activity and antigenicity of DS 22 were maintained after reduction and alkylation by iodoacetamide. The randomly folded material apparently recovered most of its native conformation by spontaneous reoxidation through dialysis against water. This was indicated by the recovery of the molecular immunopotency, ultraviolet spectral profiles, and electrophoretic characteristics. The findings suggest that the allergenic activity of DS 22 is not directly determined by the stereochemical configuration of the protein molecules but by the sequence of certain amino acids.
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