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Molecular characterization of a lectin, BPL-4, from the marine green alga Bryopsis plumosa (Chlorophyta)

  • Han, Jong-Won (Department of Biology, Kongju National University) ;
  • Yoon, Kang-Sup (Laboratory for Algae Research and Biotechnology, Arizona State University) ;
  • Jung, Min-Gui (Department of Biology, Kongju National University) ;
  • Chah, Kyong-Hwa (Department of Biology, Kongju National University) ;
  • Kim, Gwang-Hoon (Department of Biology, Kongju National University)
  • Received : 2011.12.28
  • Accepted : 2012.02.27
  • Published : 2012.03.15

Abstract

A novel lectin specific to N-acetyl-D-galactosamine as well as N-acetyl-D-glucosamine was isolated from Bryopsis plumosa and named as BPL-4. Sodium dodecyl sulfate polyacrylamide gel electrophorese (SDS-PAGE) and matrix-assisted laser desorption / ionization-time of flight (MALDI-TOF) mass spectrometry data showed that this lectin was a monomeric protein with molecular weight 12.9 kDa. The N-terminal amino acid sequences of the lectin were determined by Edman degradation and the full cDNA sequence encoding this lectin was obtained using the degenerate primers designed from the amino acid sequence. The size of the cDNA was 414 bp containing single open reading frame (ORF) encoding the lectin precursor. The homology analysis showed that this lectin might belong to H lectin group. BPL-4 showed high sequence similarity (60.6%) to BPL-3, which is a previously reported lectin from the same species. The comparative analysis on the lectin's primary structure showed two conserved domains including one possible active domain of H lectin group.

Acknowledgement

Supported by : National Research Foundation of Korea

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