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Affinity Purification of Recombinant Galectins

  • Jun Iwaki
  • Jun Hirabayashi

Abstract

Galectins are multifunctional animal lectins defined as β-galactoside-binding proteins with conserved carbohydrate-recognition domains (CRDs). They are largely classified into three structural types: proto, chimera, and tandem-repeat types (Kasai and Hirabayashi 1996). The proto- and chimera-type galectins are composed of a single CRD and form noncovalent multimers, typically dimer of prototype ones. On the other hand, the tandemrepeat type galectins consist of two distinct CRDs connected by a linker polypeptide. Most galectins exhibit hemagglutinin activity inhibited by β-galactosides, such as lactose.

Keywords

Luria Bertani Xylanase Activity Galectin Expression Molecular Mass Marker Amicon Ultra 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Bailey MJ, Biely P, Poutanen K (1992) Interlaboratory testing of methods for assay of xylanase activity. J Biotech 23:257–270CrossRefGoogle Scholar
  2. Kasai K, Hirabayashi J (1996) Galectins: a family of animal lectins that decipher glycocodes. J Biochem (Tokyo) 119:1–8 (Review)Google Scholar
  3. Levi G, Teichberg VI (1981) Isolation and physicochemical characterization of electrolectin, a β-d-dgalactoside binding lectin from electric organ of Electrophorus electricus. J Biol Chem 256:5735–5740PubMedGoogle Scholar

Copyright information

© Springer 2008

Authors and Affiliations

  • Jun Iwaki
    • 1
  • Jun Hirabayashi
    • 1
  1. 1.Lectin Application and Analysis Team, Research Center for Medical GlycoscienceNational Institute of Advanced Industrial Science and TechnologyUmezono, Tsukuba, IbarakiJapan

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