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

@article{Kawsar2008IsolationPC,
  title={Isolation, purification, characterization and glycan-binding profile of a d-galactoside specific lectin from the marine sponge, Halichondria okadai.},
  author={Sarkar Mohammad Abe Kawsar and Yuki Fujii and Ryo Matsumoto and Takayuki Ichikawa and Hiroaki Tateno and Jun Hirabayashi and Hidetaro Yasumitsu and Chikaku Dogasaki and Masahiro Hosono and Kazuo Nitta and Jiharu Hamako and Taei Matsui and Yasuhiro Ozeki},
  journal={Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology},
  year={2008},
  volume={150 4},
  pages={
          349-57
        }
}
A lectin recognizing both Galbeta1-3GlcNAc and Galbeta1-4GlcNAc 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… CONTINUE READING
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