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The Properties of Thyroglobulin

XIII. THE STRUCTURE OF REDUCED ALKYLATED THYROGLOBULIN

From the ¹ From the Clinical Endocrinology Branch, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland 20014

All the disulfide bonds of thyroglobulin have been completely reduced with ß-mercaptoethanol in urea or guanidine at alkaline pH. The molecular properties of reduced carboxymethylated thyroglobulin have been investigated in aqueous solution by sedimentation velocity, viscosity, difference spectra, optical rotation, polarization of fluorescence, electrophoresis, spectrophotometric titration, and Ouchterlony gel diffusion. These methods indicate that the reduced form of thyroglobulin is a two-chain molecule which is comparable in rigidity to the native form, although differing significantly in being highly permeated by solvent. It is suggested that the form of the molecule may be envisioned as similar to that of a sponge.

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