Biologically Active Monoiodinated Salmon Calcitonin Purified by Polyacrylamide Gel Electrophoresis

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Abstract
125I and 131I salmon calcitonin (sCT) have been purified by polyacrylamide gel electrophoresis. This technique enabled complete separation of labeled from native molecules. Radioimmunoassay of the same amounts of radioactivity before and after purification showed that the specific activity obtained (610 and 575 μCi/μg as a mean for 125I and 131I, respectively) corresponded to the theoretical specific activity for one atom of iodine per molecule (533 for 125I and 667 μCi/μg for 131I). The purified hormone was 90% bound by an excess of specific antibody and retains full biological potency.