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Partial Purification of Rat Serum Thyroxine-Binding Globulin

  • Masataka Nanno
  • Rieko Ohtsuka
  • Noriyuki Kikuchi
  • Yutaka Oki
  • Shozo Ohgo
  • Hiroyuki Kurahachi
  • Teruya Yoshimi
  • Satoshi Hamada

Abstract

Rats have been frequently used experimentally in various aspects of thyroid research, but their serum-binding proteins for thyroid hormones (TH) remain unclear compared with those of human beings. Previous studies showed that in rats the major serum TH-binding protein was electrophoretically slow migrating prealbumin (R-TBPA) (1). Davis et al. (2) reported the presence of rat serum thyroxine-binding globulin (R-TBG) using polyacrylamide gel slab electrophoresis, but other studies showed little or no R-TBG (3,4). In special conditions such as on feeding rats a low protein, high carbohydrate diet (4) or on fasting (5), the rats were reported to gain clear R-TBG band. Thus, R-TBG has not yet been purified, and its binding characteristics have not been determined. We report that R-TBG was partially purified using Sephadex G-200 gel filtration from hypothyroid rat serum and its binding characteristics determined by charcoal-binding method.

Keywords

Binding Characteristic High Carbohydrate Diet Relative Affinity Maximal Binding Capacity Charcoal Adsorption 
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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References

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Copyright information

© Springer Science+Business Media New York 1986

Authors and Affiliations

  • Masataka Nanno
    • 1
  • Rieko Ohtsuka
    • 1
  • Noriyuki Kikuchi
    • 1
  • Yutaka Oki
    • 1
  • Shozo Ohgo
    • 1
  • Hiroyuki Kurahachi
    • 1
  • Teruya Yoshimi
    • 1
  • Satoshi Hamada
    • 1
  1. 1.Second Department of Internal Medicine, Hamamatsu University School of MedicineHamamatsu and Tenri HospitalTenriJapan

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