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Effect of Oleate, Diphenylhydantoin, and Heparin on the Binding of ¹²⁵I-Thyroxine to Purified Thyroxine-Binding Globulin

Department of Biochemistry, New York Medical College Fifth Avenue at 106th Street, New York, New York 10029

The effect of oleate, diphenylhydantoin, and heparin on the binding of ¹²⁵I-thyroxine to highly purified human thyroxine-binding globulin (TBG) has been studied. Oleate was about twice as effective as diphenylhydantoin in displacing ¹²⁵I-thyroxine from TBG as ascertained by starch gel electrophoresis at pH 8.6. In vitro addition of heparin was relatively ineffective in inhibiting thyroxine (T4) binding to TBG. The possible physiological significance of the results lies in the observation that oleate inhibited T4- binding to TBG at molar ratios to T4 that were well within the normal range (free fatty acid: T4) existing in plasma.

This research was supported by NIH Grant AM-05344.

¹ Requests for reprints should be sent to Dr. Milton Tabachnick, Department of Biochemistry, New York Medical College, Fifth Avenue at 106th Street, New York, N.Y. 10029.

² 2Permanent address: American National Red Cross, Blood Research Laboratory, 9312 Old Georgetown Road, Bethesda, Maryland 20014.

Received June 5, 1972.

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