Purification and Characterization of T3-Receptor from Beef Liver Plasma Membrane

  • Ryuya Horiuchi
  • Kiyoshi Yamauchi
  • Sakuji Koya
  • Hiroo Takikawa


Over the past two decades, it has been believed that the transport of thyroid hormones into cells was by simple diffusion. However, recent evidence indicates that the uptake of T3 into the cells occurs by receptor-mediated endocytosis (1), and that this mode of entry is physiologically significant (2). It is also known that the plasma membrane receptor is highly stereospecific for L-T3 (3). Two classes of T3-receptor (high affinity - low capacity and low affinity - high capacity sites) were determined in GH3 cells (3), swiss 3T3 cells (4) and human erythrocytes (5). Using affinity labeling with Bromoacetyl [125I]T3 (BrAc[125I]T3, the binding site of the T3-receptor was identified by SDS-PAGE to be a 55K dalton band (3). However, its structural details and the role of the plasma membrane receptor on the mechanism of T3 action have not been clearly defined.


Coomassie Blue Staining Plasma Membrane Receptor Imidazole Buffer Affinity Label Amino Acid Component 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Science+Business Media New York 1986

Authors and Affiliations

  • Ryuya Horiuchi
    • 1
  • Kiyoshi Yamauchi
    • 1
  • Sakuji Koya
    • 1
  • Hiroo Takikawa
    • 1
  1. 1.Institute of EndocrinologyGunma UniversityMaebashiJapan

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