Investigation of the effect of denaturation on certain chemical, physicochemical, and biological properties of proteins has proved a valuable approach in the study of protein structure. Further advances have been made by a study of the reversal of the process of denaturation and by comparative measurements of the properties of a protein in the native and regenerated 1 states. Recently, evidence has been given to show that the denaturation of horse serum albumin (2) and of pseudoglobulin (3) by urea and guanldine hydrochloride are essentially irreversible processe s (4-6) although the regenerated proteins simulate certain characteristic properties of the native materials from which they were derived.