Purification and Characterization of a New Galactoside Specific Lectin from Trichosanthes kirilowii Root

  • Yun, Doo-Hee (Department of Food Science and Technology, Kyungsung University) ;
  • Park, Eun-Ju (Department of Food Science and Technology, Kyungsung University) ;
  • Park, Jong-Ok (Department of Chemistry, Kyungsung University) ;
  • Lee, Young-Han (Department of Life Science, Pohang University of Science and Technology) ;
  • Seo, Jeong-Kon (Department of Life Science, Pohang University of Science and Technology) ;
  • Ryu, Sung-Ho (Department of Life Science, Pohang University of Science and Technology) ;
  • Suh, Pann-Ghill (Department of Life Science, Pohang University of Science and Technology) ;
  • Kim, Hee-Sook (Department of Food Science and Technology, Kyungsung University)
  • Received : 0
  • Accepted : 0
  • Published : 0

Abstract

A new lectin, named TRA, was purified from Trichosanthes kirilowii root by acid-treated Sepharose 6B, Mono-Q, and TSK-gel 3000SW column sequential chromatography. The lectin appeared homogeneous by native gel electrophoresis at pH 4.3 and gave two protein bands of Mr=31 and 28 kDa by SDS-PAGE. The N-terminal amino acid sequences of the polypeptides of TRA have not been reported in amino acid sequences of the lectins. TRA lectin formed a precipitate with asialofetuin, neuraminidase-treated fetuin. A sugar inhibition assay indicated that N-acetyl-D-galactosamine, among the monosaccharides tested, was the most potent inhibitor of TRA-induced hemagglutination. Asialofetuin showed a 260-times stronger inhibitory activity than N-acetyl-D-galactosamine. TRA lectin also showed agglutination with normal leukocytes and lymphoma cells, but not with premature hemopoietic cells. These results suggest that TRA is a novel plant lectin.

Keywords

Lectin;TRA;asialofetuin;hemagglutination;hemopoietic cell