THE PURIFICATION OF BEEF THYROGLOBULIN WITH THE USE OF GEL FILTRATION
L. Perelmutter, W F Devlin, N. R. Stephenson
Abstract
L. Perelmutter, W F Devlin, N. R. Stephenson
Abstract
A method is described for preparing a 19 S thyroglobulin component from a saline beef thyroid extract by chromatographic fractionation on Sephadex G-200. By employing Sephadex G-200 it was possible to separate a saline extract of minced beef thyroid gland into several fractions, the first of which (fraction I) contained approximately 60% of the protein and 96% of the iodine. Spectrophotometric, ultracentrifugal, and immunochemical methods revealed that fraction I possessed, in addition to the 19 S thyroglobulin protein, a 25 S component as well as serum proteins. A narrow band of fraction I appeared to be free of both the 25 S component and the serum proteins. The material in this subfraction had a sedimentation constant of S20,w = 19.1 and contained 1.2 mg of iodine per 100 mg of protein.
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A method is described for preparing a 19 S thyroglobulin component from a saline beef thyroid extract by chromatographic fractionation on Sephadex G-200. By employing Sephadex G-200 it was possible to separate a saline extract of minced beef thyroid gland into several fractions, the first of which (fraction I) contained approximately 60% of the protein and 96% of the iodine. Spectrophotometric, ultracentrifugal, and immunochemical methods revealed that fraction I possessed, in addition to the 19 S thyroglobulin protein, a 25 S component as well as serum proteins. A narrow band of fraction I appeared to be free of both the 25 S component and the serum proteins. The material in this subfraction had a sedimentation constant of S20,w = 19.1 and contained 1.2 mg of iodine per 100 mg of protein.
Key concepts: Thyroglobulin, Sephadex, Chromatography, Chemistry, Fractionation, Iodine, Size-exclusion chromatography, Fraction (chemistry)