Studies on human thyroxine-binding globulin (TBG)

Abstract

A method for obtaining highly purified thyroxine-binding globulin (TBG) from whole human serum is presented. The method employs relatively simple procedures of step-wise ammonium sulfate precipitation followed by column chromatography on DEAE cellulose and DEAE Sephadex. The final product produces a single protein band on disc electrophoresis. The sedimentation constant of the TBG thus purified is 3.91 and its calcu-

Familial thyroxine-binding globulin deficiency: search for linkage with Xg blood groups

“…As the methods used in most studies have depended on the binding of isotope-labelled thyroxine to identify TBG, a protein with low affinity for thyroxine would not have been detected. Marshall and Pensky (1969), using immunodiffusion methods, found that both normal and TBG-deficient serum contained two proteins which reacted with an antiserum raised against a preparation of serum TBG. However, in subsequent studies using a more specific radioimmunoassay method, Levy, Marshall, and Velayo (1971) were unable to detect TBG in 'TBG-deficient' serum and concluded that the earlier findings may have been due to lack of specificity of the antiserum.…”