SynopsisThyroglobulins were extracted from the thyroid glands of one amphibia (Xenopus laevis), one ayes (chicken) and five mammals (whale, rat, hog, monkey and human), and purified by means of salting-out with ammonium sulfate followed by DEAE-cellulose chromatography. Sedimentation coefficients, electrophoretic mobilities, isoelectric points, immunochemical properties as well as iodine contents and amino acid compositions of all or most of these thyroglobulins were determined and the results were compared with each other. In spite of a great variety of animal species studied, these thyroglobulins were found to be rather similar in various respects, while species specificity was clearly indicated. Most distinct differences were observed among amphibian, avian and mammalian thyroglobulins, especially in amino acid composition, isoelectric point and immunochemical properties.