TY - JOUR
T1 - Isolation, purification, characterization and glycan-binding profile of a d-galactoside specific lectin from the marine sponge, Halichondria okadai
AU - Kawsar, Sarkar M.A.
AU - Fujii, Yuki
AU - Matsumoto, Ryo
AU - Ichikawa, Takayuki
AU - Tateno, Hiroaki
AU - Hirabayashi, Jun
AU - Yasumitsu, Hidetaro
AU - Dogasaki, Chikaku
AU - Hosono, Masahiro
AU - Nitta, Kazuo
AU - Hamako, Jiharu
AU - Matsui, Taei
AU - Ozeki, Yasuhiro
PY - 2008/8
Y1 - 2008/8
N2 - 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.
AB - 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.
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U2 - 10.1016/j.cbpb.2008.04.004
DO - 10.1016/j.cbpb.2008.04.004
M3 - Article
C2 - 18534886
AN - SCOPUS:45849146139
SN - 1096-4959
VL - 150
SP - 349
EP - 357
JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
IS - 4
ER -