Guinea pig thyroglobulin (19 S) shows a time-dependent dissociation into half-sized (12 S) subunits at neutral pH in 0.1 M KCl. The reaction is completely reversible between 1 and 23° and is endothermic since higher temperature favors the 19 S species. The rate and equilibrium of association have been measured by light scattering and velocity centrifugation, respectively. Increasing the salt concentration increases the rate and the equilibrium constant of association. The velocity constant of association is strongly dependent on pH, decreasing rapidly as the pH is raised from 6.4 to 8.4. The degree of dissociation of guinea pig thyroglobulin increases with decreasing iodine content.
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Schneider et al. (1970) studied this question.
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