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The presence of a specific thyroxine-binding protein in human serum was first suggested from studies by Gordon, Gross, O'Connor, and PittRivers (1), employing zone electrophoresis. Although such a protein has not yet been isolated, certain of its properties may be determined in unfractionated serum when the specific protein has been labeled with thyroxine-I'11. In this way, it has been demonstrated that this protein has: 1) an electrophoretic mobility at pH 8.6 (1-5), as well as at pH 6 and 7.6 (5), intermediate between alpha-i and alpha-2 globulins, 2) an electrophoretic mobility at pH 4.5 similar to the "M-2 proteins," or alpha-2 glycoproteins, of serum (6), and 3) a sedimentation rate in the ultracentrifuge of approximately 3.3 Svedbergs (7). In the present study, this technique has been applied to an investigation of the thyroxine-binding capacity of this specific protein.

THYROXINE-BINDING CAPACITY OF SERUM IN NORMAL MAN 1