THYROXINE-SERUM PROTEIN COMPLEXES: TWO-DIMENSION GEL AND PAPER ELECTROPHORESIS STUDIES

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Abstract
Two dimensional (paper-paper and paper-gel) electrophoresis of human scrum containing labeled thyroxine has been performed with various buffers. Thyroxinc-bindingprealbumin (TBPA), as seen in paper electrophoresis in ammonium carbonate buffer, appears to be identical with the fastest moving thyroxine zone (band 1) in starch gel electrophoresis in borate buffer. Albuminbound thyroxine in ammonium carbonate or barbital buffer appears in starch gel as band 2 and a band migrating slower than band 4 the identity of which has not been established. The albumin separated on starch gel appears to be non-homogeneous with respect to its thyroxine binding. Thyroxine-binding alpha globulin (TBG) in ammonium carbonate and barbital buffer is seen in starch gel as band 4. In paper electrophoresis using barbital buffer, TBPA probably migrates ahead of albumin although a prealbumin component also appears to migrate with the alpha globulin. However, relatively high concentrations of barbital appear to inhibit binding of thyroxine by TBPA. TBG in barbital and carbonate are identical. Band 3 in starch gel has not been identified.

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