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

Yasuhiro Ozeki, Taei Matsui, Kazuo Nitta, Hiroaki Kawauchi, Yoshio Takayanagi, Koiti Titani

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30 Citations (Scopus)


A β-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 soluble 14kDa β-galactoside-binding lectins (14K-lectin) widely distributed in vertebrates and classified as S type lectins. These results indicate that a 14K-lectin is present as the free form in unfertilized frog eggs, presenting the first structural evidence for the presence of a soluble 14K-lectin in the amphibian eggs.

Original languageEnglish
Pages (from-to)407-413
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 15-07-1991
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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