IMMUNOCHEMICAL PROPERTIES OF THYROID PROTEINS

Abstract

Saline extracts obtained from both beef and hog thyroid glands were chromatographed on Sephadex G-200. An ultracentrifugal and immunochemical examination of the fractions showed that subfractions which possessed the 19 S component and a sufficient concentration of the 25 S component gave rise to two precipitin bands by the agar gel diffusion technique. Immunoelectrophoretic studies indicated that these antigens migrated in the region of α2globulins. In addition, it was found that subfractions which contained both the 19 S and 25 S components had higher extinction coefficients at 280 mμ and lower OD280/OD260ratios than those in which the 19 S component occurred alone. From these results, it can be suggested that the 19 S and 25 S components have different immunochemical and spectrophotometric properties.