Expression and characterization of the recombinant human galectin-3

유전자 재조합 Human galectin-3의 발현과 성상

  • Kim, Byung-gyu (College of Veterinary Medicine, Seoul National University) ;
  • Woo, Hee-jong (College of Veterinary Medicine, Seoul National University)
  • 김병규 (서울대학교 수의과대학) ;
  • 우희종 (서울대학교 수의과대학)
  • Received : 1997.05.13
  • Published : 1997.09.25


Galectin-3 is known as an animal ${\beta}$-galactoside-binding lectin charicterized with S-type carbohydrate recognition domain. It plays a role in growth, adherence and movement of cells. It is, also, related to the cell transformation and metastasis of tumor cells. In this study, we have expressed and purified recombinant human galectin-3 (rHgalectin-3) using E coli system and asialofetuin affinity chromatography for the future development of monoclonal antibody to Hgalectin-3, which is suggested as the tumor marker for the gastric and thyroid gland cancers. Expressed protein was confirmed as the Hgalectin-3 by immunoblot with cross-reactive murine monoclonal antibody. Lectin activity and specificity of purified protein were, also, confirmed by the competitive inhibition with galectin-3 specific carbohydrate, lactose. Like physiological galectin-3, lectin activity of the molecule was not changed in nonreduced condition. Dimer formation, furthermore, was observed at high concentration of the protein even in the reduced condition, which is well known in physiological galectin-3. These results showed purified rHgalectin-3 has the same activity and molecular nature compared to the physiological galectin-3.


Supported by : 한국학술진흥재단