Isolation, purification, characterization and glycan-binding profile of a d-galactoside specific lectin from the marine sponge, Halichondria okadai

Sarkar M.A. Kawsar, Yuki Fujii, Ryo Matsumoto, Takayuki Ichikawa, Hiroaki Tateno, Jun Hirabayashi, Hidetaro Yasumitsu, Chikaku Dogasaki, Masahiro Hosono, Kazuo Nitta, Jiharu Hamako, Taei Matsui, Yasuhiro Ozeki

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

A lectin recognizing both Galβ1-3GlcNAc and Galβ1-4GlcNAc was purified from the demosponge Halichondria okadai by lactosyl-agarose affinity chromatography. The molecular mass of the lectin was determined to be 30 kDa by SDS-PAGE under reducing and non-reducing conditions and 60 kDa by gel permeation chromatography. The pI value of the lectin was 6.7. It was found to agglutinate trypsinized and glutaraldehyde-fixed rabbit and human erythrocytes in the presence and absence of divalent cations. The hemagglutinating activity by the lectin was inhibited by d-galactose, methyl-d-galactopyranoside, N-acetyl-d-galactosamine, methyl-N-acetyl-d-galactosaminide, lactose, melibiose, and asialofetuin. The Kd of the lectin against p-nitrophenyl-β-lactoside was determined to be 2.76 × 10- 5 M and its glycan-binding profile given by frontal affinity chromatography was shown to be similar to many other known galectins. Partial primary structure analysis of 7 peptides by cleavage with lysyl endopeptidase indicated that one of the peptides showed significant similarity with galectin purified from the sponge Geodia cydonium.

Original languageEnglish
Pages (from-to)349-357
Number of pages9
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume150
Issue number4
DOIs
Publication statusPublished - 08-2008

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Molecular Biology

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