Date of Award

7-1963

Document Type

Thesis - Restricted

Degree Name

Master of Science (MS)

Department

Medical

First Advisor

E.A. Birge

Second Advisor

J.M. Lubitz

Third Advisor

L.J. Van Hecke

Abstract

Hamolsky, Goldetz and Freedberg, in the discussion which accompanied their original work, felt that the erythrocyte uptake of tri-iodothyronine was a reflection of the incorporation of thyroid hormone by the peripheral tissues. It has been well demonstrated that thyroxine (T4),, the. major circulating thyroid hormone, is bound to a more or less specific protein moiety. This protein has been called the thyroid binding protein or thyroid binding globulin (TBG). This protein migrates electrophoretically between alpha-1 and alpha-2 globulin at pH 8.5. Other investigators have noted that tri-iodothyronine (T3) is bound to protein in a similar manner. This bond is less complete and less firm, than the binding of T4. Lesser amounts of thyroxine are bound to albumin, and this protein serves as a secondary carrier, especially when the levels of thyroid hormone are increased.

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