Purification, characterization, and sugar binding specificity of an N-Glycolylneuraminic acid-specific lectin from the mushroom Chlorophyllum molybdites.

@article{Kobayashi2004PurificationCA,
  title={Purification, characterization, and sugar binding specificity of an N-Glycolylneuraminic acid-specific lectin from the mushroom Chlorophyllum molybdites.},
  author={Yuka Kobayashi and Kouji Kobayashi and Kanako Umehara and Hideo Dohra and Takeomi Murata and Taichi Usui and Hirokazu Kawagishi},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 51},
  pages={53048-55}
}
A carbohydrate-binding protein was isolated from the carpophores of the mushrooms and designated the Chlorophyllum molybdites lectin (CML) based on its origin. The molecular mass of CML was 32 kDa, and it was composed of two 16-kDa monomers with no disulfide bonds. Monosaccharide analysis indicated that 12% of the mass of CML was carbohydrate and consisted of GlcNAc:GalNAc:Gal:Man:l-Fuc in a molar ratio of 1.5:1.9: 4.4:4.8:1.0. In the hemagglutination inhibition assay, CML exhibited the… CONTINUE READING

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