Purification and characterization of beta-galactoside binding lectin from frog (Rana catesbeiana) eggs.

@article{Ozeki1991PurificationAC,
  title={Purification and characterization of beta-galactoside binding lectin from frog (Rana catesbeiana) eggs.},
  author={Yohei Ozeki and Toshitaka Matsui and Katsutoshi Nitta and Hiroshi Kawauchi and Yuki Takayanagi and Koiti Titani},
  journal={Biochemical and biophysical research communications},
  year={1991},
  volume={178 1},
  pages={407-13}
}
A beta-galactoside-binding lectin, a homodimer composed of 14kDa subunits, was purified from unfertilized eggs of the frog Rana catesbeiana by asialofetuin-Sepharose 4B affinity column chromatography. The lectin was solubilized from eggs by addition of neither haptenic sugar nor detergent and showed a unique characteristic that it requires neither Ca++ nor SH-reagent for its hemagglutination activity. However, the partial amino acid sequence indicated that the lectin belongs to a family of… CONTINUE READING

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